Phosphorylation of Bacillus subtilis gene regulator AbrB modulates its DNA-binding properties

• AbrB is a global gene regulator involved in transition phase phenomena in Bacillus 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 S86D leads to a significant loss of AbrB control over several key target functions: exoprotease production, competence development and sporulation. A wider transcriptome analysis of abrBS86D and S86A 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.

Subject headings

NATURVETENSKAP  -- Biologi -- Biologisk systematik (hsv//swe)

NATURAL SCIENCES  -- Biological Sciences -- Biological Systematics (hsv//eng)

Keyword

RAUCH MA

1997

1995

V179

MOLECULAR MICROBIOLOGY

V177

TRANSITION-STATE REGULATOR

DOMAIN

V246

APRE EXPRESSION

EMBO JOURNAL

eilly M

P522

RAUCH MA

TRANSCRIPTION

P1203

P1615

V8

TYROSINE

PROMOTER

RAUCH MA

JOURNAL OF BACTERIOLOGY

MOLECULAR & GENERAL GENETICS

JOURNAL OF BACTERIOLOGY

RAUCH MA

V3

1995

1989

SPORULATION

SPECIFICITY

P756

P6999

1989

MYCOBACTERIUM-TUBERCULOSIS

PROTEIN-KINASES

Publication and Content Type

art (subject category)

ref (subject category)