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The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54.
Proc Natl Acad Sci U S A. 2003 Mar 04; 100(5):2278-83.PN

Abstract

Members of the protein family called ATPases associated with various cellular activities (AAA(+)) play a crucial role in transforming chemical energy into biological events. AAA(+) proteins are complex molecular machines and typically form ring-shaped oligomeric complexes that are crucial for ATPase activity and mechanism of action. The Escherichia coli transcription activator phage shock protein F (PspF) is an AAA(+) mechanochemical enzyme that functions to sense and relay the energy derived from nucleoside triphosphate hydrolysis to catalyze transcription by the sigma(54)-RNA polymerase. Closed promoter complexes formed by the sigma(54)-RNA polymerase are substrates for the action of PspF. By using a protein fragmentation approach, we identify here at least one sigma(54)-binding surface in the PspF AAA(+) domain. Results suggest that ATP hydrolysis by PspF is coupled to the exposure of at least one sigma(54)-binding surface. This nucleotide hydrolysis-dependent presentation of a substrate binding surface can explain why complexes that form between sigma(54) and PspF are transient and could be part of a mechanism used generally by other AAA(+) proteins to regulate activity.

Authors+Show Affiliations

Department of Biological Sciences, Sir Alexander Fleming Building, Imperial College London, South Kensington Campus, London SW7 2AZ, United Kingdom.No affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info availableNo affiliation info available

Pub Type(s)

Journal Article
Research Support, Non-U.S. Gov't

Language

eng

PubMed ID

12601152

Citation

Bordes, Patricia, et al. "The ATP Hydrolyzing Transcription Activator Phage Shock Protein F of Escherichia Coli: Identifying a Surface That Binds Sigma 54." Proceedings of the National Academy of Sciences of the United States of America, vol. 100, no. 5, 2003, pp. 2278-83.
Bordes P, Wigneshweraraj SR, Schumacher J, et al. The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54. Proc Natl Acad Sci U S A. 2003;100(5):2278-83.
Bordes, P., Wigneshweraraj, S. R., Schumacher, J., Zhang, X., Chaney, M., & Buck, M. (2003). The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54. Proceedings of the National Academy of Sciences of the United States of America, 100(5), 2278-83.
Bordes P, et al. The ATP Hydrolyzing Transcription Activator Phage Shock Protein F of Escherichia Coli: Identifying a Surface That Binds Sigma 54. Proc Natl Acad Sci U S A. 2003 Mar 4;100(5):2278-83. PubMed PMID: 12601152.
* Article titles in AMA citation format should be in sentence-case
TY - JOUR T1 - The ATP hydrolyzing transcription activator phage shock protein F of Escherichia coli: identifying a surface that binds sigma 54. AU - Bordes,Patricia, AU - Wigneshweraraj,Siva R, AU - Schumacher,Jörg, AU - Zhang,Xiaodong, AU - Chaney,Matthew, AU - Buck,Martin, Y1 - 2003/02/24/ PY - 2003/2/26/pubmed PY - 2003/5/14/medline PY - 2003/2/26/entrez SP - 2278 EP - 83 JF - Proceedings of the National Academy of Sciences of the United States of America JO - Proc Natl Acad Sci U S A VL - 100 IS - 5 N2 - Members of the protein family called ATPases associated with various cellular activities (AAA(+)) play a crucial role in transforming chemical energy into biological events. AAA(+) proteins are complex molecular machines and typically form ring-shaped oligomeric complexes that are crucial for ATPase activity and mechanism of action. The Escherichia coli transcription activator phage shock protein F (PspF) is an AAA(+) mechanochemical enzyme that functions to sense and relay the energy derived from nucleoside triphosphate hydrolysis to catalyze transcription by the sigma(54)-RNA polymerase. Closed promoter complexes formed by the sigma(54)-RNA polymerase are substrates for the action of PspF. By using a protein fragmentation approach, we identify here at least one sigma(54)-binding surface in the PspF AAA(+) domain. Results suggest that ATP hydrolysis by PspF is coupled to the exposure of at least one sigma(54)-binding surface. This nucleotide hydrolysis-dependent presentation of a substrate binding surface can explain why complexes that form between sigma(54) and PspF are transient and could be part of a mechanism used generally by other AAA(+) proteins to regulate activity. SN - 0027-8424 UR - https://www.unboundmedicine.com/medline/citation/12601152/The_ATP_hydrolyzing_transcription_activator_phage_shock_protein_F_of_Escherichia_coli:_identifying_a_surface_that_binds_sigma_54_ L2 - http://www.pnas.org/cgi/pmidlookup?view=long&pmid=12601152 DB - PRIME DP - Unbound Medicine ER -