Seavers, P.R., Lewis, R.J., Brannigan, J.A. et al. (3 more authors) (2001) Structure of the Bacillus cell fate determinant SpoIIAA in phosphorylated and unphosphorylated forms. Structure, 9 (7). pp. 605-614. ISSN 0969-2126
Abstract
Background: The asymmetric cell division during sporulation in Bacillus subtilis gives rise to two compartments: the mother cell and the forespore. Each follow different programs of gene expression coordinated by a succession of alternate RNA polymerase σ factors. The activity of the first of these σ factors, σF, is restricted to the forespore although σF is present in the predivisional cell and partitions into both compartments following the asymmetric septation. For σF to become active, it must escape from a complex with its cognate anti-σ factor, SpoIIAB. This relief from SpoIIAB inhibition requires the dephosphorylation of the anti-σ factor antagonist, SpoIIAA. The phosphorylation state of SpoIIAA is thus a key determinant of σF activity and cell fate.
Results: We have solved the crystal structures of SpoIIAA from Bacillus sphaericus in its phosphorylated and unphosphorylated forms. The overall structure consists of a central β-pleated sheet, one face of which is buried by a pair of α helices, while the other is largely exposed to solvent. The site of phosphorylation, Ser57, is located at the N terminus of helix α2. The phosphoserine is exceptionally well defined in the 1.2 Å electron density maps, revealing that the structural changes accompanying phosphorylation are slight.
Conclusions: Comparison of unphosphorylated and phosphorylated SpoIIAA shows that covalent modification has no significant effect on the global structure of the protein. The phosphoryl group has a passive role as a negatively charged flag rather than the active role it plays as a nucleus of structural reorganization in many eukaryotic signaling systems.
Metadata
Item Type: | Article |
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Authors/Creators: |
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Dates: |
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Institution: | The University of York |
Academic Units: | The University of York > Faculty of Sciences (York) > Chemistry (York) |
Depositing User: | York RAE Import |
Date Deposited: | 10 Feb 2009 15:16 |
Last Modified: | 10 Feb 2009 15:16 |
Published Version: | http://dx.doi.org/10.1016/S0969-2126(01)00623-2 |
Status: | Published |
Publisher: | Elsevier |
Identification Number: | 10.1016/S0969-2126(01)00623-2 |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:7578 |