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A novel bacterial tyrosine kinase essential for cell division and differentiation.
- Source :
-
Proceedings of the National Academy of Sciences of the United States of America [Proc Natl Acad Sci U S A] 1999 Nov 09; Vol. 96 (23), pp. 13068-73. - Publication Year :
- 1999
-
Abstract
- Protein kinases play central roles in the regulation of eukaryotic and prokaryotic cell growth, division, and differentiation. The Caulobacter crescentus divL gene encodes a novel bacterial tyrosine kinase essential for cell viability and division. Although the DivL protein is homologous to the ubiquitous bacterial histidine protein kinases (HPKs), it differs from previously studied members of this protein kinase family in that it contains a tyrosine residue (Tyr-550) in the conserved H-box instead of a histidine residue, which is the expected site of autophosphorylation. DivL is autophosphorylated on Tyr-550 in vitro, and this tyrosine residue is essential for cell viability and regulation of the cell division cycle. Purified DivL also catalyzes phosphorylation of CtrA and activates transcription in vitro of the cell cycle-regulated fliF promoter. Suppressor mutations in ctrA bypass the conditional cell division phenotype of cold-sensitive divL mutants, providing genetic evidence that DivL function in cell cycle and developmental regulation is mediated, at least in part, by the global response regulator CtrA. DivL is the only reported HPK homologue whose function has been shown to require autophosphorylation on a tyrosine, and, thus, it represents a new class of kinases within this superfamily of protein kinases.
- Subjects :
- Amino Acid Sequence
Base Sequence
Cell Differentiation genetics
Cell Division genetics
DNA Primers
Molecular Sequence Data
Mutagenesis, Site-Directed
Phosphorylation
Protein-Tyrosine Kinases chemistry
Protein-Tyrosine Kinases genetics
Transcription, Genetic
Tyrosine physiology
Caulobacter crescentus enzymology
Cell Differentiation physiology
Cell Division physiology
Protein-Tyrosine Kinases physiology
Subjects
Details
- Language :
- English
- ISSN :
- 0027-8424
- Volume :
- 96
- Issue :
- 23
- Database :
- MEDLINE
- Journal :
- Proceedings of the National Academy of Sciences of the United States of America
- Publication Type :
- Academic Journal
- Accession number :
- 10557274
- Full Text :
- https://doi.org/10.1073/pnas.96.23.13068