page_title: Transcription activator-like effector
hierarchical_section_title: Transcription activator-like effector
caption_attribution_description: English: Space-filling drawing of a TAL effector bound to double-helical DNA. TALE proteins contain a series of alpha-helical hairpin domains, each of which binds an individual DNA base, so that the protein recognizes a long, very specific DNA sequence. Plant bacteria can use a TALE protein to target transcription of a specific gene that makes the plant more susceptible to infection. Drawn by David Goodsell from PDB file 3UGM.
context_page_description: TAL effectors are proteins secreted by Xanthomonas bacteria via their type III secretion system when they infect various plant species. These proteins can bind promoter sequences in the host plant and activate the expression of plant genes that aid bacterial infection. They recognize plant DNA sequences through a central repeat domain consisting of a variable number of ~34 amino acid repeats. There appears to be a one-to-one correspondence between the identity of two critical amino acids in each repeat and each DNA base in the target sequence. These proteins are interesting to researchers both for their role in disease of important crop species and the relative ease of retargeting them to bind new DNA sequences. Similar proteins can be found in the pathogenic bacterium Ralstonia solanacearum and Burkholderia rhizoxinica, as well as yet unidentified marine microorganisms. The term TALE-likes is used to refer to the putative protein family encompassing the TALEs and these related proteins.
context_section_description: TAL (transcription activator-like) effectors (often referred to as TALEs, but not to be confused with the three amino acid loop extension homeobox class of proteins) are proteins secreted by Xanthomonas bacteria via their type III secretion system when they infect various plant species.  These proteins can bind promoter sequences in the host plant and activate the expression of plant genes that aid bacterial infection.  They recognize plant DNA sequences through a central repeat domain consisting of a variable number of ~34 amino acid repeats.   There appears to be a one-to-one correspondence between the identity of two critical amino acids in each repeat and each DNA base in the target sequence.  These proteins are interesting to researchers both for their role in disease of important crop species and the relative ease of retargeting them to bind new DNA sequences.  Similar proteins can be found in the pathogenic bacterium Ralstonia solanacearum and Burkholderia rhizoxinica, as well as yet unidentified marine microorganisms. The term TALE-likes is used to refer to the putative protein family encompassing the TALEs and these related proteins.
caption: TAL effector (PDB: 3ugm​), spacefill by David Goodsell. Stripes are repeat domains.
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