期刊
NUCLEIC ACIDS RESEARCH
卷 42, 期 8, 页码 5177-5190出版社
OXFORD UNIV PRESS
DOI: 10.1093/nar/gku146
关键词
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资金
- BBSRC [BB/H011234/1, BB/H012249/1, BB/J002828/1, BB/G001278/1]
- University of Leeds
- Wellcome Trust [062164, 090932/Z/09/Z, WT093044MA]
- RC UK
- Biotechnology and Biological Sciences Research Council [BB/K000233/1, BB/G001278/1, BB/J002828/1, BB/E000975/1, BB/H011234/1, BB/H012249/1] Funding Source: researchfish
- Wellcome Trust [100958/Z/13/Z] Funding Source: researchfish
- BBSRC [BB/K000233/1, BB/H011234/1, BB/J002828/1, BB/E000975/1, BB/G001278/1, BB/H012249/1] Funding Source: UKRI
- MRC [MR/J006874/1] Funding Source: UKRI
Recognition of bacterial promoters is regulated by two distinct classes of sequence-specific sigma factors, sigma(70) or sigma(54), that differ both in their primary sequence and in the requirement of the latter for activation via enhancer-bound upstream activators. The sigma(54) version controls gene expression in response to stress, often mediating pathogenicity. Its activator proteins are members of the AAA+ superfamily and use adenosine triphosphate (ATP) hydrolysis to remodel initially auto-inhibited holoenzyme promoter complexes. We have mapped this remodeling using single-molecule fluorescence spectroscopy. Initial remodeling is nucleotide-independent and driven by binding both ssDNA during promoter melting and activator. However, DNA loading into the RNA polymerase active site depends on co-operative ATP hydrolysis by the activator. Although the coupled promoter recognition and melting steps may be conserved between sigma(70) and sigma(54), the domain movements of the latter have evolved to require an activator ATPase.
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