Structural basis for recognition of AT-rich DNA by unrelated xenogeneic   silencing proteins

doi:10.1073/pnas.1102544108

CORC > 北京大学 > 化学与分子工程学院

	Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins
	Gordon, Blair R. G. ; Li, Yifei ; Cote, Atina ; Weirauch, Matthew T. ; Ding, Pengfei ; Hughes, Timothy R. ; Navarre, William Wiley ; Xia, Bin ; Liu, Jun
刊名	proceedings of the national academy of sciences of the united states of america
	2011
关键词	NUCLEOID-ASSOCIATED PROTEIN NS-LIKE PROTEINS LATERAL GENE-TRANSFER H-NS ESCHERICHIA-COLI MINOR-GROOVE RNA-POLYMERASE MYCOBACTERIUM-TUBERCULOSIS YERSINIA-ENTEROCOLITICA PREFERENTIALLY BINDS
DOI	10.1073/pnas.1102544108
英文摘要	H-NS and Lsr2 are nucleoid-associated proteins from Gram-negative bacteria and Mycobacteria, respectively, that play an important role in the silencing of horizontally acquired foreign DNA that is more AT-rich than the resident genome. Despite the fact that Lsr2 and H-NS proteins are dissimilar in sequence and structure, they serve apparently similar functions and can functionally complement one another. The mechanism by which these xenogeneic silencers selectively target AT-rich DNA has been enigmatic. We performed high-resolution protein binding microarray analysis to simultaneously assess the binding preference of H-NS and Lsr2 for all possible 8-base sequences. Concurrently, we performed a detailed structure-function relationship analysis of their C-terminal DNA binding domains by NMR. Unexpectedly, we found that H-NS and Lsr2 use a common DNA binding mechanism where a short loop containing a "Q/RGR" motif selectively interacts with the DNA minor groove, where the highest affinity is for AT-rich sequences that lack A-tracts. Mutations of the Q/RGR motif abolished DNA binding activity. Netropsin, a DNA minor groove-binding molecule effectively outcompeted H-NS and Lsr2 for binding to AT-rich sequences. These results provide a unified molecular mechanism to explain findings related to xenogeneic silencing proteins, including their lack of apparent sequence specificity but preference for AT-rich sequences. Our findings also suggest that structural information contained within the DNA minor groove is deciphered by xenogeneic silencing proteins to distinguish genetic material that is self from nonself.; Multidisciplinary Sciences; SCI(E); 0; ARTICLE; 26; 10690-10695; 108
语种	英语
内容类型	期刊论文
源URL	[http://ir.pku.edu.cn/handle/20.500.11897/394718]
专题	化学与分子工程学院
推荐引用方式 GB/T 7714	Gordon, Blair R. G.,Li, Yifei,Cote, Atina,et al. Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins[J]. proceedings of the national academy of sciences of the united states of america,2011.
APA	Gordon, Blair R. G..,Li, Yifei.,Cote, Atina.,Weirauch, Matthew T..,Ding, Pengfei.,...&Liu, Jun.(2011).Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins.proceedings of the national academy of sciences of the united states of america.
MLA	Gordon, Blair R. G.,et al."Structural basis for recognition of AT-rich DNA by unrelated xenogeneic silencing proteins".proceedings of the national academy of sciences of the united states of america (2011).