TAL Effectors Specificity Stems from Negative Discrimination
نویسندگان
چکیده
منابع مشابه
TAL Effectors Specificity Stems from Negative Discrimination
Transcription Activator-Like (TAL) effectors are DNA-binding proteins secreted by phytopathogenic bacteria that interfere with native cellular functions by binding to plant DNA promoters. The key element of their architecture is a domain of tandem-repeats with almost identical sequences. Most of the polymorphism is located at two consecutive amino acids termed Repeat Variable Diresidue (RVD). T...
متن کاملSupporting Information Material for TAL effectors specificity stems from negative discrimination
Table of Content SUPPORTING METHODS ...................................................................................................................... 2 Set-up and simulation protocol for molecular dynamics ................................................................ 2 Binding energy calculations ..............................................................................................
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Xanthomonas spp. are Gram-negative bacteria with powerful molecular weapons to attack their plant hosts. Key for pathogenicity of Xanthomonas is a type III secretion system that injects a cocktail of effector proteins into plant cells to function as potent virulence factors. TAL (transcription activator-like) effectors from Xanthomonas function as transcriptional activators of plant genes in th...
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TAL effectors are proteins secreted by bacterial pathogens into plant cells, where they enter the nucleus and activate expression of individual genes. TAL effectors display a modular architecture that includes a central DNA-binding region comprising a tandem array of nearly identical repeats that are almost all 34 residues long. Residue number 13 in each TAL repeat (one of two consecutive polym...
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AvrBs3, the founding member of the Xanthomonas transcription-activator-like effectors (TALEs), is translocated into the plant cell where it localizes to the nucleus and acts as transcription factor. The DNA-binding domain of AvrBs3 consists of 17.5 nearly-identical 34 amino acid-repeats. Each repeat specifies binding to one base in the target DNA via amino acid residues 12 and 13 termed repeat ...
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ژورنال
عنوان ژورنال: PLoS ONE
سال: 2013
ISSN: 1932-6203
DOI: 10.1371/journal.pone.0080261