DOI: 10.5061/dryad.6djh9w1dj
title: Data for: Mechanistic insights into TTLL11 polyglutamylase-mediated primary tubulin chain elongation

description: Microtubules (MTs) undergo diverse posttranslational modifications that
 regulate their structural and functional properties. Among these,
 polyglutamylation—a dominant and conserved modification targeting
 unstructured tubulin C-terminal tails—plays a pivotal role in defining the
 tubulin code. Here, we describe a mechanism by which tubulin tyrosine
 ligase–like 11 (TTLL11) expands and diversifies the code. Cryo–electron
 microscopy revealed a unique bipartite MT recognition strategy wherein
 TTLL11 binding and catalytic domains engage adjacent MT protofilaments.
 Biochemical and cellular assays identified previously uncharacterized
 polyglutamylation patterns, showing that TTLL11 directly extends the
 primary polypeptide chains of α-and β-tubulin in vitro, challenging the
 prevailing paradigms emphasizing lateral branching. Moreover, cell-based
 and in vivo data suggest a cross-talk between polyglutamylation and the
 detyrosination/tyrosination cycle likely linked to the TTLL11-mediated
 elongation of the primary α-tubulin chain. These findings unveil an
 unrecognized layer of complexity within the tubulin code and offer
 mechanistic insights into the molecular basis of functional specialization
 of MT cytoskeleton.
description: # Data for: Mechanistic insights into TTLL11 polyglutamylase-mediated
 primary tubulin chain elongation Dataset DOI:
 [10.5061/dryad.6djh9w1dj](10.5061/dryad.6djh9w1dj) ## Description of the
 data and file structure All data were acquired to describe the structure
 and functions of TTLL11 polyglutamylase. Many methods were used, including
 cryo-EM, mass spectrometry, TIRF microscopy, and cell-based assays.  ###
 Files and variables #### File: TTLL11_MT_complex_structure_(1).zip
 **Description:** model of the TTLL11/microtubules complex and the
 deposition protocol from the RCSB database #### File:
 cryosparc_P35_J257_006_volume_map_hancer_highRes.mrc **Description:** map
 of the TTLL11/microtubules complex from cryo-EM #### File: 18O.zip
 **Description:** MS data of glutamylation by TTLL11 and 18O labeled
 glutamate #### File: TIRF_TTLL11_variants.zip **Description:** TIRF
 microscopy image of TTLL11 variants binding to microtubules #### File:
 fragmentation_data_hMTs.zip **Description:** mass spectrometry data of
 TTLL11 glutamylated human microtubules of beta tubulin #### File:
 alpha_d3.zip **Description:** mass spectrometry data of TTLL11
 glutamylated delta3 microtubules #### File: immunofluor_intens.zip
 **Description:** data from fluorescence microscopy of neurons #### File:
 alpha_detyr.zip **Description:** mass spectrometry data of TTLL11
 glutamylated detyrosinated microtubules #### File: alpha_HEK_MTs.zip
 **Description:** mass spectrometry data of TTLL11 glutamylated human
 microtubules of alpha tubulin #### File: alpha_Tyr.zip
 **Description:** mass spectrometry data of TTLL11 glutamylated tyrosinated
 microtubules #### File: fragmentation_data.zip **Description:** tandem
 mass spectrometry data of glutamylated tubulin ends #### File:
 beta_tubulin_d2d3.zip **Description:** mass spectrometry data of TTLL11
 glutamylated human microtubules of truncated beta tubulin #### File:
 beta_tubulins.zip **Description:** mass spectrometry data of TTLL11
 glutamylated human microtubules of beta tubulin ## Code/software ImageJ -
 fluorescence microscopy data ChimeraX - structural data Data Analysis
 (Bruker) - mass spectrometry data - not free, mmass can be used instead
 for quantification data ## Access information Other publicly accessible
 locations of the data: * structural data - PDB ID 9HQ4 and EMD-52338 at
 [www.rcsb.org/](http://www.rcsb.org/) and
 [www.ebi.ac.uk/emdb/](http://www.ebi.ac.uk/emdb/)