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

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].

所属期刊栏目：22

资助基金：We are grateful to the staff at Beamline BL17U at Shanghai Synchrotron Radiation FacilitySSRF,Chinafor help with data collection.This work was supported by the State Key Program of National Natural Science of China31130063;Chinese Ministry of Science and Technology2010CB835300;the National Outstanding Young Scholar Science Foundation of National Natural Science Foundation of China20101331722.The atomic coordinates have been deposited in the Protein Data Bankaccession code 4HPZ

在线出版日期：2013-03-15（万方平台首次上网日期，不代表论文的发表时间）

页数：共5页

页码：1716-1720