4.7 Article

The anti-σ factor SpoIIAB forms a 2:1 complex with σF, contacting multiple conserved regions of the σ factor

期刊

JOURNAL OF MOLECULAR BIOLOGY
卷 300, 期 1, 页码 17-28

出版社

ACADEMIC PRESS LTD- ELSEVIER SCIENCE LTD
DOI: 10.1006/jmbi.2000.3838

关键词

anti-sigma; Bacillus subtilis; Bacillus stearothermophilus; sigma factor; transcription

资金

  1. NIGMS NIH HHS [GM53759] Funding Source: Medline

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The developmental regulatory protein sigma(F) of Bacillus subtilis, a member of the sigma(70)-family of bacterial RNA polymerase sigma factors, is negatively reguL lated by the anti-sigma factor SpoIIAB, which binds to sigma(F), sequestering it in an inactive complex. SpoIIAB binding to sigma(F) is strongly stimulated by ATP. Here, we use a combination of gel filtration chromatography, dynamic light-scattering, analytical ultracentrifugation, limited proteolysis with N-terminal sequencing and electrosyray mass spectrometry, and deletion analysis to probe the SpoIIAB-sigma(F) complex. The studies were facilitated by investigating the homologs from Bacillus stearothermophilus as well as co-expression of the proteins in Escherichia coli, allowing purification of large quantities of the in vivo assembled complex. We determined the stoichiometry of the complex to be SpoIIAB(2):sigma(1)(F). Alone, sigma(F) is rapidly degraded by the protease trypsin. In the complex with SpoIIAB, however, sigma(F) is remarkably resistant to proteolysis. Analysis of the protease cleavage data indicates the anti-sigma binds sigma(F) through contacts with multiple conserved regions of the sigma factor, supporting previous findings based on genetic data. (C) 2000 Academic Press.

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