The DNA-binding domain in the Bacillus subtilis transition-state regulator AbrB employs significant motion for promiscuous DNA recognition

被引:22
作者
Vaughn, JL
Feher, VA
Bracken, C
Cavanagh, J
机构
[1] Purdue Univ, Dept Chem, W Lafayette, IN 47907 USA
[2] SUNY Albany, Dept Biol Sci, Albany, NY 12222 USA
[3] Cornell Univ, Weill Med Coll, Dept Biochem, New York, NY 10021 USA
关键词
dynamics; AbrB; transition-state regulator; DNA-binding;
D O I
10.1006/jmbi.2000.4305
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
AbrB is a Bacillus subtilis protein responsible for regulating a diverse array of unrelated genes during periods of sub-optimal growth conditions. DNA binding by AbrB is unique in that sequence recognition is specific, yet no obvious consensus sequence of bound promoter regions is apparent. The N-terminal domain is a recently characterized representative of a novel class of DNA-binding proteins that possess a looped hinge helix DNA-binding topology. Although the structural characterization of this DNA-binding topology contributed to an understanding of the architectural basis for recognition of DNA target sequences, specific mechanisms responsible for promiscuity in DNA sequence recognition still were not apparent. Analysis of N-15 backbone relaxation parameters shows that dynamic motion of regions directly linked to DNA binding show concerted motion on the microsecond-millisecond timescale. Furthermore, dynamic motion of the hinge region suggests that the DNA-binding region is capable of conformational orientations that allow it to accommodate DNA sequence variability in the cognate binding sites. (C) 2001 Academic Press.
引用
收藏
页码:429 / 439
页数:11
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