Crystal structure of a TALE protein reveals an extended N-terminal DNA binding region

• 来源期刊: 细胞研究（英文版）
• 年，卷（期）: 2012,（12）
• 页码范围: 1716-1720
• 页数: 5页
• 语种: 英文
• DOI: 10.1038/cr.2012.156

摘要

Dear Editor,Xanthomonas TALEs(transcription activator-like effectors)are modular proteins characterized by an Nterminal T3S signal(T3SS),a central tandem repeat domain,C-terminal nuclear localization signals(NLSs)and an acidic transcriptional activation domain(AD)[1-3].The central tandem repeats are nearly identical and are typically composed of 34 highly conserved amino acids,containing repeat-variable diresidues(RVDs)at the 12th and 13th positions that mediate their DNA binding specificity[1-5].More than 20 types of RVDs have been identified thus far,among which HD,NG,NI and NN are the four most common ones with a specificity for the nucleotides C,T,A and G/A,respectively[4,5].