Journal
MOLECULAR CELL
Volume 9, Issue 3, Pages 527-539Publisher
CELL PRESS
DOI: 10.1016/S1097-2765(02)00470-7
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Funding
- NCRR NIH HHS [RR00862] Funding Source: Medline
- NIGMS NIH HHS [GM53759, GM20470] Funding Source: Medline
- NATIONAL CENTER FOR RESEARCH RESOURCES [P41RR000862] Funding Source: NIH RePORTER
- NATIONAL INSTITUTE OF GENERAL MEDICAL SCIENCES [R01GM053759] Funding Source: NIH RePORTER
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The sigma subunit is the key regulator of bacterial transcription. Proteolysis of Thermus aquaticus sigma(A), which occurred in situ during crystallization, reveals three domains, sigma(2), sigma(3), and sigma(4), connected by flexible linkers. Crystal structures of each domain were determined, as well as Of sigma(4) complexed with -35 element DNA. Exposed surfaces of each domain are important for RNA polymerase binding. Universally conserved residues important for -10 element recognition and melting lie on one face Of sigma(2), while residues important for extended -10 recognition lie on sigma(3). Genetic studies correctly predicted that a helix-turn-helix motif in sigma(4) recognizes the -35 element but not the details of the protein-DNA interactions. Positive control mutants in sigma(4) cluster in two regions, positioned to interact with activators bound just upstream or downstream of the -35 element.
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