Talk:Flagellum

message: 1) The flagella and the intelligent design debate is not correct. No one claims the "only function properly when all proteins are in place" The case is "only function properly when all parts are in place. The parts are the: stator, rotor, shaft, bushing. hook and whip are in place. Changing the word part to protein is dishonest. 
Even if one uses the proteins, not the parts, the debate is still not correct, it is like saying "a car still runs if the air filter and muffler are removed" Removing not needed proteins-parts is irrelative. Removing extra parts that are not used to make the engine run is not irreducibly complex. The stator, rotor, shaft, bushing. hook and whip all must be in place for flagella to work.
2) The "vestigial flagella" is a part in an algae not bacterial, so this in not correct.
Telecine Guy (talk) 21:19, 25 December 2017 (UTC)
thread_title: Flagella and the intelligent design debate, proteins or parts

message: However, all non-dividing eukaryotic cells contain a flagellum (or cilium), not only sperm cells. Stationary cells (such as kidney, intestine, and nerve cells) also contain flagella (cilia) which project from the cell body out into the extracellular environment.
This sounds inexact, to say the least. SaintCahier 02:30, 3 August 2007 (UTC)
thread_title: Is this True?

message: From the Bacterial flagellum section:
:A shaft runs between the hook and the basal body, passing through protein rings in the cell's membrane that act as bearings.
From Basal Body:  (Bold added)
:A basal body is an organelle formed from a centriole, a short cylindrical array of microtubules. It is found at the base of a eukaryotic cell cilium or flagellum and serves as a nucleation site for the growth of the axoneme microtubules. Basal bodies anchor cilia.
One or the other must be incorrect in some regard.
As the wiki-link isn't working:    Abramul 22:10, 1 April 2007 (UTC)
thread_title:  Basal body as part of bacterial flagellum? 

message: At a quick look this article seems to have no refs!Osborne 15:27, 19 June 2007 (UTC)
replies: text: Wikipedia has some biology-related articles with no references and others that have many dozens of references....it generally depends on experts doing some work on pages in their area. I like the idea of having a page in Wikipedia for every protein.....making new articles that explain each protein is one way to move some of the details out of the more general articles. Also, if you ever feel like you are going beyond basic encyclopedia articles or into original research, feel free to move over to other projects like Wikibooks and Wikiversity (Wikiversity even allows some forms of original research). If you have not been there, take a look at Wikipedia:WikiProject Molecular and Cellular Biology and some of the other "wikiprojects". There are templates and tricks already in use for linking to many of the online biology databases. --JWSchmidt (talk) 02:46, 4 January 2008 (UTC)
thread_title: References

message: It would be very helpful if someone knowledgeable about the subject matter could create a diagram of the flagellum mechanism.  I know my way around Inkscape and would be happy to collaborate if needed; just ping my talk page.  Thanks!  --Sean 19:40, 5 September 2007 (UTC)
thread_title:  Diagram? 

message: Took the freedom to add an underline to that picture of a gram-negative flagellum, and furthermore moved it from the chapter Eukaryotic flagellum to the chapter, well, Bacterial flagellum. Thought that might make more sense.
I hereby propose to add the picture from the artice "Cilium" here, as eukaryotic flagella and eukaryotic cilia share the same construction (except for the length).
Your friendly neighboorhood nerd 87.169.61.234 20:54, 30 November 2007 (UTC)
thread_title:  Picture accuracy

message: Describe the chemotaxis systems of bacteria
Bacteria require motility to move towards nutrients such as sugars and to approach regions of favourable temperatures, pH, light and osmolarity. They must also move away from unfavourable conditions, such as ionising radiation, and extremes of temperature, pH or osmolarity. Bacteria must sense these conditions and integrate the corresponding signals to adjust their motility appropriately. All characterised motile bacteria respond to moving away from favourable conditions by perturbing their motility.
	Due its medical importance, its ease of growth, and the ease of which it can be assayed, E. coli has been studied as a model system for chemotaxis. Hence, this essay will be describing E. coli, except where mentioned otherwise. The chemotactic ability of E.coli can be assayed by monitoring the rate at which a colony of bacteria will spread on a nutrient plate. By using this assay to scree for mutants, a range of mutants were identified:
Dead								(due to unrelated proteins)
Non motile							(Fli mutants)
Non-responsive to any repellents or attractants	(Che mutants)
Non responsive to particular attractant or repellent	(receptor mutants)
	The Fli mutants were found to encode proteins that formed the bacterial flagellum. The swimming of bacteria can be observed under a light microscope, and recorded by high speed cinematography. From this, bacteria are seen to move by rotating rigid flagella. Bacteria are also seen to have multiple flagella, which align when swimming forwards. The flagellum was seen to generate a waveform, indicating a cyclical rotation of the flagellum, which could drive the bacteria forwards. The direction of waveform was seen to intermittently change, which causes the flagella to move apart and cause the bacterium to tumble. The  current interpretation of this is described below.
	The flagellum is made up of a transmembrane motor complex that traverses the inner and outer membranes, and a long rigid flagellum that is connected to the transmembrane region by a hook. The transmembrane region is around 45nm in diameter and the flagellum is around 10μm in length.
	The flagellum is a polymer of FliC (aka flagellin) monomers with a central cavity. Flagellin has two conformations in its polymeric form, a right handed helix and a left handed helix. This has been shown by low resolution EM studies of mutants that are trapped into a particular handedness, and by molecular dynamics simulations of the wild type form.
	In smooth swimming mode, flagellin forms a right handed helix (R), and the motor is rotated anticlockwise. When bacteria move into a region of lower favourability, the motor switches to clockwise rotation, which places a strain on the flagellum. This strain induces a change in handedness of the helix to a left handed form (L). Then, upon resumption of anticlockwise rotation, the bacteria will tumble, hence changing the direction in which the bacterium resumes swimming.
	The hook is made up of around of 120 FliE monomers. It serves to mechanically transmit the rotation of the motor to the rotation of the flagellum, without the motor moving laterally in the membrane, and without the flagellum pivoting relative to the bacterium. In order to achieve this, it has both a good degree of flexibility and structural integrity.
	The motor is complrised of transmembrane MS ring, a C ring that is positioned on the cytoplasmic side of the inner membrane and and outer ring of transmembrane stator proteins. The stator proteins have been visualised by freeze fracture electron microscopy, which shows them in an outer ring. The effect of mutations in the MotA protein of the stator can be suppressed by mutations in FliG or FliN, which suggests that MotA interacts with FliG and FliN. The relative orientations of the protein have been shown by low resolution EM.
	The MS ring is comprised of FliF subunits and it thought to act as a scaffold for the insertion of other proteins. This is because it is the first protein to be inserted into the membrane, it is centrally positioned in the motor, and it lacks any other known function.
	 Rotation of the flagellum can be disrupted by inhibition of the electron transport chain and uncoupler's of charge or protons. Also, suppressors of ATP levels (DCCD and arsenate) did not have such an effect on rotation. This suggested that rotation is energetically driven by the proton gradient and not ATP hydrolysis. The ability of MotA to translocate H+ in reconstituted vesicles suggested that MotA is the protein that couples H+ translocation into movement of the motor.
	Homology modelling suggests that MotA has four transmembrane helices and a peptidoglycan domain. Cross-linking experiments show that MotA interacts with MotB, a protein with single transmembrane helix. Together, MotA and MotB proteins form the stator ring.
	MotB has a conserved aspartate at residue 32 that is required for rotation. Mutants of MotB were generated with different charges at residue 32, and these were expressed with MotA. MotA was treated with proteases, and the pattern of MotA fragments produced was dependant of the charge of the residue at position 32. From this, it has been proposed that MotA can respond to protonation of asp32 of MotB by undergoing a large conformational change. Furthermore, these conformational changes could drive the rotation of the motor via interactions with FliG.
	In bacteria that use a sodium motive force as opposed to a proton motive force, the stator proteins PomA/B translocate Na+, which drives the rotation. PomA/B can be expressed with a motor from a H+ translocating flagellum that lacks MotAB, and restore rotation. This suggests that the structural mechanisms for rotation are the same for both flagella.
	The C ring contains FliG and FliN (which interact with MotA) and FliM. FliM mediates the switching of the motor (by an unknown mechanism) in response to binding phosphorylated CheY.
	A mutant FliM was characterised that caused a higher probability of rotational direction switching. This mutant FliM was expressed from a plasmid in a bacterium that had endogenous CheY activity suppressed. The proportion of mutant FliM protein in the motor was correlated with the probability of switching. It was found that initially, there was little increase in probability of switching with increased mutant FliM. However, when the majority of FliM proteins in the motor were mutant, the probability of switching increased rapidly. This suggests cooperativity between FliM proteins in vivo, such that when a threshold of CheY-P proteins are bound, the motor will switch more rapidly.
	The generation of Che-P is controlled by sensory signalling systems, which are highly adept at their function. A number of signals must be integrated, such as nutrients, pH, light and osmolarity. These systems are shown to be sensitive to a changes in concentration of a few molecules over 5-7 orders of magnitude.
	Due to the small size of bacteria (around 3μm), bacteria cannot sense concentration gradients spatially. However, they are able to detect temporal changes in conditions. If conditions are improving, the generation of CheY-P is repressed. If conditions are worsening, the generation of CheY-P is promoted and switching will occur. In both cases, the sensory system must adapt, so that it becomes sensitive to changes from the current conditions.
	The sensory receptors of bacteria can be either membrane bound or cytoplasmic. Receptors were identified form mutants that were unresponsive to a particular stimulus. Membrane bound receptors are called methyl accepting chemotaxis proteins (MCP's) and have been characterised more extensively than cytoplasmic proteins. There are four characterised MCP's in E. coli:
Name
Substrate
Tar
aspartate
Tsr
serine, pH, high temperatures
Trg
ribose, galactose
Tap
dipeptides
A complete structure of an MCP has been reconstructed from structures of its constituent domains.
Domain
Source of structure
Structure
Ligand binding
Crystal from Tar
4 helix bundle per monomer
Transmembrane
Homology modelling
2 helices per monomer
HAMP
NMR
4 parallel helices per dimer
Cytoplasmic
Tsr crystal
4 helix coiled coil per dimer.
The receptor forms a dimer in vivo, and is thought to act as a trimer of dimers. The cytoplasmic domain contains membrane proximal methylatable helices and a distal signalling domain. The chain forms a hairpin loop, such that the distal end of the domain C terminus is located close to the HAMP domain. There is a CheA and a CheW binding site at the membrane-distal end of the cytoplasmic domain, and a CheR binding motif (NWETF) at the C terminus of the protein.
	CheAY is a two component system, where CheA is bound to signalling domains on receptors and CheY is the response regulator.  From the structure of the ligand binding domain, transmembrane helices and HAMP domain of MCP's, a mechanism for CheA activation has been proposed. It is thought that ligand binding can induce α2 of the ligand binding domain to pivot on its long axis, which can drive pivoting of αII of the HAMP domain on its long axis. This can drive pivoting of the cytoplasmic domain relative to the membrane, which is proposed to mediate transautophosphorylation of CheA dimers. Binding of attractants has been found to suppress CheA activation, whereas binding of repellents has been found to promote CheA activation. Hence, increases in attractant concentration and decreases in repellent concentration promote smooth swimming.
	CheA-P has five domains, named P1-P5:
P1 - Phosphate accepting domain		(contains conserved His)
P2 - response regulator binding domain	(CheY, CheB binding)
P3 - dimerisation
P4 - kinase domain				(binds ATP)
P5 - regulatory domain			(has tandem SH3 repeats)
CheA dimerisation requires P3:P3 contacts. Upon activation, a signal is received via the P5 domain, which is somehow transmitted to the P2 domain. Mutants lacking the P5 domain are constitutively active. Next, the kinase domain phosphorylates a histidine on α2 of the P1 domain of the adjacent monomer. Kinase activity is Mg2+ dependant. This phosphate can then phosphotransfer to either CheY or CheB.
	CheY is a single domain response regulator. It is activated by phosphotransfer from CheA onto a conserved Asp57. It can also undergo acetylation on lysine residues, which promotes switching, but not binding to FliM. The interpretation is that lysine acetylation has a post-binding effect on FliM. The FliM binding site on CheY has been mapped by genetic mutants and NMR. Those residues that perturb switching behaviour when mutated are seen to undergo significant chemical shifts when phosphorylated.
	CheY has intrinsic phosphatase activity with a half life of around 2 seconds. However, in vivo CheY is seen to dephosphorylate with a half life of 200ms, which is mediated by a phosphatase CheZ. It is possible that switching probability can be modulated by regulating CheZ. For example, under reducing conditions, CheZ is seen to bind CheA and promote phosphatase activity.
	CheB is a methylesterase and an acetylesterase that is activated by phosphotransfer. CheB is able to deacetylate glutamine residues on receptors, generating glutamate residues that are able to accept methyl groups. CheB also demethylates methylglutamate residues, which represses further activation of the receptor. Hence, CheB is responsible for dampening the sensitivity of the receptor upon receptor activation, which makes the receptor responsive to a threshold that is close to the current situation.
	CheB has an N terminal acceptor domain and a C terminal catalytic domain, which contains a modified Asp/His/Ser catalytic triad. The crystal structures of the active and inactive forms show little difference between the active and inactive forms for the C terminal domain, but flexibility in the N terminal domain. In the unphosphorylated state, the NTD is seen to block access to the active site, and phosphorylation is thought to induce a conformational change that relieves this inhibition.
	CheR is a constitutively active methyltransferase that methylates receptors. It acts antagonistically to CheB and serves to increase the sensitivity of a receptor to activation. This works with CheR to adjust the threshold required to induce switching to the current levels of attractant and repellent.
	CheR binds to NWETF motifs on receptors, which serves to localise CheR to the methylation sites on said receptors. Mutagenesis of CheR and the Tar receptor suggested that binding required negatively charged residues on Tar and positively charged residues on α2 of CheR. This strongly suggests that the binding is electrostatically mediated. CheR uses S-adenosyl-methionine as a methyl donor.
	One of the observations of the chemotaxis sensing system is that it is sensitive to tiny temporal changes in receptor concentration over 5-7 orders of magnitude. Adaptation of the receptor proteins can account for the range over which receptors can sense changes. However, the observed sensitivity of the signalling system is far better than that expected for independently acting receptors. In part, this can be accounted for by the cooperativity proposed between FliM proteins. Also, the concept of large scale receptor coupling has been proposed.
	GFP tagging of chemotactic receptors in Rhodobacter sphaeroides  has shown receptors to form clusters at cytoplasm and at the cell poles. A number of mathematical models for inducing signal propagation and hence chemotactic gain have been proposed. One such model is a variation of the Monod, Wyman and Changeux model, in which the the cluster can exist in either a T state or an R state. When a threshold is reached, i.e. when enough receptors have repellents bound and few have attractants bound, the probability of moving from a T state to an R state increases, and causes CheA activation.
	Receptor clustering requires CheA and CheW proteins, as shown by the lack of clustering of GFP-tagged receptors in CheW and CheA deficient cells. The stoichiometry of the signalling clusters is thought to be:
3 receptor dimers : 3 CheA monomers : 3 CheW monomers
However, the arrangement of proteins within the clusters is unknown.
	All bacterial and archaeal chemotaxis systems characterised to date appear to be divergently related. Although the same principles apply in each case, some subtle variations on the E. coli system have been found.
	In B. subtilis, the CheAY two component system is activated under opposite circumstances, but has opposite effect. Increases in attractant binding and reductions in repellent binding cause CheA to autophosphorylate, and  CheY-P to bind FliM and repress switching.
	In E. coli, methylation at different sites can be induced by any receptor and each methylation causes equivalent effects. However, methylation in B. subtilis is site-specific, such that methylation at a particular site occurs in response to a particular event. At some sites, methylation is induced in response to an increase in attractants and at other sites in response to a decrease.
	CheR from B. subtilis uses methanol as a substrate for methylation and is a product of demethylation. This use of reductant may be energetically costly for the cell, and so at low levels of attractant, a different system is used. This involves CheA-P phosphotransfer to CheV, which is a CheW-CheY fusion protein.
	CheC and CheD have also been implicated in adaptation. CheC is involved in CheY-P dephosphorylation and hence signal termination.
	In Rhodobacter sphaeroides, there are two distinct chemotaxis pathways that are encoded by different operon's. These operon's are expressed to different degrees, depending on the oxygen concentration.
	R. sphaeroides has two sets of clusters, namely nine MCP's in the membrane and four Tlp's (transducer-like-proteins) in the cytosol. Additionally, it has four CheA isoforms and six CheY isoforms. Each CheA has a range of CheY specificities, and the reason for this is unknown.
	Rhizobium meliloti responds to different chemotactic stimuli not by inducing switching, but by modulating flagella speed. It has two CheY isoforms:
CheY1 - acts as a phosphate sink for CheY2
CheY2 - reduces speed of flagella rotation
By labelling CheA with 32[P]ATP, CheA was shown to phosphotransfer to both CheY1 and CheY2. However, when CheY1 and CheY2 were labelled with 32[P]phosphates, only CheY2 was able to perform retrograde phosphotransfer back to CheA. Hence, CheY1 acts as a phosphate sink that enhances the dephosphorylation of CheY2. The intrinsic phosphatase activities of both proteins were shown to have half lives of around 10s, and no CheZ was present.
The movement of phosphates is shown below:
	Although some holes in our understanding remain, the chemotaxis system in E.coli has been well characterised from the binding of attractant to the mechanism of propulsion. Further work is required to understand the structural basis of CheA activation and the basis of cooperativity in signalling clusters. From the lessons learned in E.coli, we will be better able understand the chemotaxis systems of other organisms.  —Preceding unsigned comment added by 84.71.66.130 (talk) 11:00, 4 April 2008 (UTC)
thread_title:  chemotaxis etc

message: I really don't see a problem with having a brief paragraph about Michael Behe's claim that the bacterial flagellum could not have evolved, and the subsequent rejection of this claim by the scientific community and demonstration that it is not irreducibly complex. Can anybody explain what's the objection to this? Please speak up. <eleland/talkedits> 14:36, 4 May 2008 (UTC)
replies: text: Personally, I rather think that it's a good idea to include such a section. The flagellum is, after all, one of his primary examples of so-called "irreducible complexity". – ClockworkSoul 14:45, 4 May 2008 (UTC)
replies: text: I think the version that we use, however, should be a little more graceful than this edit, though. The irony quotes are a bit over the top. – ClockworkSoul 14:54, 4 May 2008 (UTC)
replies: text: You have a point there. <eleland/talkedits> 18:12, 4 May 2008 (UTC)

text: I kind of agree, but from the opposite direction: the ID section isn't too long, the rest of the article is too short, and needs some real editing love. As for irony, as an encyclopedia we have to strive for neutrality, regardless of how we feel about the subject. – ClockworkSoul 22:02, 11 May 2008 (UTC)
replies: text: I agree about shortening the ID section. I think it doesn't deserve so much attention in a scientific article. I disagree, though, about an encyclopedia being neutral in a sense that equates scientific knowledge to irrationality and superstition. I think an encyclopedia should be strongly commited to facts and reality, and even more so in a scientific article. I also think that the fact that the idea of irreducible complexity is widely rejected by the scientific community should be expressed in a clearer way and earlier in the section. Many readers may not reach the final sentence and therefore, take the wrong impression that ID is actually taken seriously by the scientific community.--Diegoarmino (talk) 15:17, 27 January 2009 (UTC)

text: I'm sort of torn. In a way this question reflects the broader debate within the scientific community about how to respond to ID and other forms of "Creation [pseudo]Science;" do you refute their arguments at the risk of giving them credibility, or ignore them at the risk of looking like you're scared to defend science? I think the section should stay more or less the length that it is. Wikipedia is a general-interest encyclopedia, and I suspect that many if not most of the casual readers for this article are looking specifically for the information about ID and evolution. For example, on the social-bookmarking site StumbleUpon, this site is summarized with "Bacteria that defies darwinian eveloution thory. Made if complex parts this bacteria is liken to a machine." <eleland/talkedits> 10:24, 18 May 2008 (UTC)
thread_title:  Behe / complexity 

message: Dare I say it? The first sentence of this article has fourteen references. That's about one reference per two or three words. Surely the entire contents of the sentence are captured in some subset of those references—one or two at most! — HorsePunchKid (talk) 2008-05-15 04:38:24Z
: I agree that citing fourteen references is excessive.  I have removed the foreign language citations since according to WP:Cite, all other things being equal, preference should be given to English language citations.  This at least reduces the number from 14 to 10.  The number should probably be reduced further, but I do not know enough about the subject to select the most appropriate of the remaining citations to keep.  Cheers.  Boghog2 (talk) 09:19, 18 May 2008 (UTC)
replies: text: If those sources are not used more than once, they could be compiled into a single <ref> to save readability. <eleland/talkedits> 10:18, 18 May 2008 (UTC)
thread_title:  Too many references? 

message: Please, someone who serves a regulatory function for Wikipedia needs to make sure scientific articles such as this one do not contain ANY material that is not cited.  I have gone through and fixed several common misconceptions regarding flagella v. cilia.  Students that have studied from the previous page have gotten misinformation regarding the differences between these structures, and it is all because some individuals think they know what they are talking about when they don't have a clue.  If citations are given, there is a great reduction in the possibility that the information is incorrect.
And to anyone adding information to the encyclopedia: Please don't cite anything that you haven't verified from a peer-reviewed scientific journal or textbook!  Don't just take the word of your teacher, friend, or a random website!!  —Preceding unsigned comment added by 208.54.95.197 (talk) 15:43, 2 June 2008 (UTC)
thread_title:  Citations Needed!!! Flagella v. Cilia. 

message: It is more than a nuisance that the same term 'flagellum'
is used in the literature for two such completly different
structures such as the eukaryotic flagellum and prokaryotic flagellum.
The article accounts for this fact by mentioning the notable differences
between the two.
I want to propose a more radical step: Why not have two articles
for the two kinds of flagella and a disambiguity page?  —Preceding unsigned comment added by 91.64.166.91 (talk) 19:01, 1 July 2008 (UTC)
replies: text: *Sounds like a good idea to me too. - Zephyris Talk 15:07, 5 April 2011 (UTC)
thread_title:  Eukaryotic flagellum and prokaryotic flagellum 

message: We've made a picture of a 9+2 flagellum, which I find better then the one, that is shown a the moment:
* Current: http://commons.wikimedia.org/wiki/File:Chlamydomonas_TEM_17.jpg
* New: http://commons.wikimedia.org/wiki/File:Flagellum_of_Chara_sp_TEM_x14000.png
Is it worth changing?
--and3k (talk) 06:33, 29 June 2009 (UTC)
replies: text: The proposed "new" EM shows the plasma membrane surrounding the axoneme, which is important in that it makes it clear that each flagellum has only one axoneme inside. However, the current EM does a much better job of showing the smaller structures such as the dynein arms and radial spokes. Based on that, I would still favor the current picture. What else about the proposed new picture makes it better, in the opinion of all you other editors of this page? --AaronM (talk) 21:22, 29 June 2009 (UTC)
replies: text: The "new" image at the link above has gone dead.  I guess this ends the discussion of which is better and why. N2e (talk) 20:47, 1 May 2010 (UTC)
thread_title:  9+2 Structure 

message: In the subsection Types, it says
"Eukaryotic flagella - those of animal, plant, and protist cells - are complex cellular projections that lash back and forth.",
while "Flagella vs Cilia", a subsection of "Eukaryotic" claims "In the case of flagella (e.g. the tail of a sperm) the motion is propeller-like.". So which is it: do Eukaryotic flagella lash back and forth or do they rotate in a propellor-like fashion?
Matthieumarechal (talk) 18:55, 19 April 2011 (UTC)
replies: text: I agree with you. I should try and remove it. --86.7.19.248 (talk) 23:34, 11 December 2011 (UTC)
thread_title:  Eukaryotic flagella: waving back and forth or rotating 

message: I reverted the delinking of terms such as prokaryote and eukaryote. Overlink does not mean that any term that some reader happens to know the meaning of, must not be linked. In fact in some contexts terms that everyone knows the meaning of also should be linked, in order to draw the reader's attention to particular connections. Plenty of readers who are not professional biologists couldn't tell a prokaryote from a protein, and plenty of young readers still need assistance, not only with actual definitions but with the associated implications. Please be more cautious in future with delinking. It is far more important that a helpful link should be available than that a redundant link should be deleted. It is not as though the article in question is burdened down with hundreds of unnecessary or duplicated links; just three links had been removed, all were in appropriate context, none was duplicated. In an article of that size even three inappropriate links would have been trivial. These three were not inappropriate. JonRichfield (talk) 11:30, 11 September 2012 (UTC)
replies: text: On the contrary, as I said in my edit summary, each of the links I deleted was a duplicate - fact, there were two links each for eukaryote and prokaryote in the first paragraph of the lead. I'm not dead set against repeated links, but they could at least be further apart. RockMagnetist (talk) 23:05, 11 September 2012 (UTC)

text: Quite all right. To avoid this kind of mistake, I often search on the word root (like "prokaryot") instead of the whole word. RockMagnetist (talk) 16:35, 12 September 2012 (UTC)
thread_title: Overlink and prokaryote/eukaryote

message: Unfortunately, the creator of this nice diagram is no longer very active. Please have a look at the discussion on commons, perhaps we can find someone else to improve it. https://commons.wikimedia.org/wiki/File_talk:Flagellum_base_diagram_en.svg Richard-of-Earth (talk) 19:38, 20 April 2015 (UTC)
thread_title:  The factual accuracy of the diagram is disputed 

message: Substituted at 15:14, 29 April 2016 (UTC)
thread_title: Assessment comment

message: Not every paragraph or section is cited as it should be.  For example the last paragraph under the "motor" section should have a citation and it does not.  All of the content in this article seemed to be relevant, with a neutral position.  A couple of the citations for this paper were pretty old, one dated back to 1981 and is no longer available online by the link provided, so this should be updated.  Courtneytackett (talk) 03:44, 1 October 2016 (UTC)
thread_title:  Needs more citations/some spelling/grammar errors 

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thread_title:  External links modified 

message: "Axial filament" redirects here from at least the spirochaete page and the search function.
This page however doesn't mention axial filaments, should a segment be added or rather a new page created about them? — Preceding unsigned comment added by SemenCloys (talk • contribs) 
: I believe this flagellum-on-the-inside thing should be mentioned in more detail on the Spirochaete page. --Artoria2e5 🌉 18:40, 7 December 2020 (UTC)
replies: text: Have redirected page to its aka Axoneme.--Iztwoz (talk) 10:21, 9 May 2021 (UTC)
thread_title:  Axial filament 

message: The current article tries to discuss two totally unrelated structures at once, resulting in a very strange structure. I propose to split out the heavily-loaded bacterial and eukaryotic sections to their own pages, leaving short overview sections similar to the one we already have for archaellum. The lead is also quite confusing, since its explanation of archaeal-type flagellum having a different name seems to imply that bact/euk "flagellums" are the same when they are not.
The naming of the eukaryotic page is pending discussion. The GO people call all of the microtuble-based swinging things "cilium", but that goes against common medical use. Undulipodium is an already-existing article we could use, but that name is so uncommon that GO doesn't even list it as a synonym. --Artoria2e5 🌉 18:38, 7 December 2020 (UTC)
replies: text: After going through GO and its refs (PMID 22118931) I am a bit interested in lumping it all into a big cilium article. The 9+2 classification is useful for the classical case, but nature seems quite defiant in general. Genetic issues show up in either type. Also see commentary in PMID 30692268. Still, having all these does not negate the notability of a conventional 9+2 motile cilium article.--Artoria2e5 🌉 23:45, 30 December 2020 (UTC)
replies: text:  Had a rethink on this and inclined to keep page as is: the page is not overly long and seems better to have all material on one page. The page could maybe be a bit better structured but it seems flagellum is still very much in use for both domains, and commonly searched; they are all basically units of locomotion - difference in mechanism is straightforwardly explainable imo. Would be willing to work on page sometime - am focused on another page at the moment. Re archaellum and archael flagellum being as common - makes no odds, one used has citation.--Iztwoz (talk) 14:58, 25 July 2021 (UTC)
thread_title:  Split by domain