Kumar, A., Brannigan, J.A. and Moran, C.P. (2004) alpha-helix E of Spo0A is required for sigma(A)- but not for sigma(H)-dependent promoter activation in Bacillus subtilis. Journal of Bacteriology. pp. 1078-1083. ISSN 0021-9193
Abstract
At the onset of endospore formation in Bacillus subtilis, the DNA binding protein Spo0A activates transcription from two types of promoters. The first type includes the spoIIG and spoIIE promoters, which are used by sigma(A)-RNA polymerase, whereas the second type includes the spoIIA promoter, which is used by RNA polymerase containing the secondary sigma factor sigma(H). Previous genetic analyses have identified specific amino acids in alpha-helix E of Spo0A that are important for activation of Spo0A-dependent, sigma(A)-dependent promoters. However, these amino acids are not required for activation of the sigma(H)-dependent spoIIA promoter. We now report the effects of additional single-amino-acid substitutions and the effects of deletions in alpha-helix E. The effects of alanine substitutions revealed one new position (239) in Spo0A that appears to be specifically required for activation of the sigma(A)-dependent promoters. Based on the effects of a deletion mutation, we suggest that alpha-helix E in Spo0A is not directly involved in interaction with sigma(H)-RNA polymerase.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Copyright, Publisher and Additional Information: | Copyright © 2004 American Society for Microbiology |
Keywords: | RESPONSE REGULATOR,TRANSCRIPTION FACTOR,SPORULATION,PHOSPHORELAY,INITIATION,BINDING,REGION |
Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | Sherpa Assistant |
Date Deposited: | 04 Mar 2005 |
Last Modified: | 27 Dec 2024 00:05 |
Published Version: | https://doi.org/10.1128/JB.186.4.1078-1083.2004 |
Status: | Published |
Refereed: | Yes |
Identification Number: | 10.1128/JB.186.4.1078-1083.2004 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:311 |