NMR studies of the sporulation protein SpoIIAA: Implications for the regulation of the transcription factor σF in Bacillus subtilis
- 1 January 2001
- journal article
- Published by Springer Nature in Journal of Biomolecular NMR
- Vol. 19 (4) , 293-304
- https://doi.org/10.1023/a:1011247523112
Abstract
SpoIIAA participates in a four-component mechanism for phosphorylation-dependent transcription control at the outset of sporulation. We report the refinement of the solution structure of SpoIIAA by using the automated iterative NOE assignment method ARIA. To complement the structural data, the protein dynamics were determined by measuring the T1, T2 and NOE of the backbone 15N-nuclei. The refined structure permits a discussion of the structural features that are important for the function of SpoIIAA in the regulation of the sporulation sigma factor σF, and for homologous regulatory pathways present in B. subtilis and in other bacilli.Keywords
This publication has 34 references indexed in Scilit:
- The STAS domain — a link between anion transporters and antisigma-factor antagonistsCurrent Biology, 2000
- Deciphering the biology of Mycobacterium tuberculosis from the complete genome sequenceNature, 1998
- Identification of communication networks in Spo0F: a model for phosphorylation‐induced conformational change and implications for activation of multiple domain bacterial response regulatorsFEBS Letters, 1998
- Structure of the CheY-binding domain of histidine kinase CheA in complex with CheYNature Structural & Molecular Biology, 1998
- NMRPipe: A multidimensional spectral processing system based on UNIX pipesJournal of Biomolecular NMR, 1995
- The program XEASY for computer-supported NMR spectral analysis of biological macromoleculesJournal of Biomolecular NMR, 1995
- Role of interactions between SpoIIAA and SpoIIAB in regulating cell-specific transcription factor σF of Bacillus subtilisGenes & Development, 1994
- Backbone Dynamics of a Free and a Phosphopeptide-Complexed Src Homology 2 Domain Studied by 15N NMR RelaxationBiochemistry, 1994
- CRYSTAL STRUCTURE OF ESCHERICHIA COLI CHEY REFINED AT 1.7-ANGSTROM RESOLUTIONPublished by Worldwide Protein Data Bank ,1993
- Crisscross regulation of cell-type-specific gene expression during development in B. subtilisNature, 1992