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Phosphorylation of B acillus subtilis gene regulator AbrB modulates its DNA-binding properties.
- Source :
-
Molecular Microbiology . Jun2014, Vol. 92 Issue 5, p1129-1141. 13p. - Publication Year :
- 2014
-
Abstract
- AbrB is a global gene regulator involved in transition phase phenomena in B acillus subtilis. It participates in a complex regulatory network governing the expression of stationary-phase functions. AbrB was previously found to be phosphorylated on serine 86 located close to its C-terminal oligomerization domain. Here we report that AbrB can be phosphorylated by three B . subtilis serine/threonine kinases expressed during the transition and stationary phase: PrkC, PrkD and YabT. Our in vitro findings suggest that AbrB phosphorylation impedes its DNA binding and abolishes binding cooperativity. In vivo we established that a phospho-mimetic mutation abrB S86 D leads to a significant loss of AbrB control over several key target functions: exoprotease production, competence development and sporulation. A wider transcriptome analysis of abrB S86 D and S86 A mutant strains revealed deregulation of a large number of target genes. We therefore propose that AbrB phosphorylation serves as an additional input for fine-tuning the activity of this ambiactive gene regulator. [ABSTRACT FROM AUTHOR]
Details
- Language :
- English
- ISSN :
- 0950382X
- Volume :
- 92
- Issue :
- 5
- Database :
- Academic Search Index
- Journal :
- Molecular Microbiology
- Publication Type :
- Academic Journal
- Accession number :
- 96210927
- Full Text :
- https://doi.org/10.1111/mmi.12617