Glutamate at the phosphorylation site of response regulator CtrA provides essential activities without increasing DNA binding
AUTOR(ES)
Siam, Rania
FONTE
Oxford University Press
RESUMO
The essential response regulator CtrA controls the Caulobacter crescentus cell cycle and phosphorylated CtrA∼P preferentially binds target DNA in vitro. The CtrA aspartate to glutamate (D51E) mutation mimics phosphorylated CtrA∼P in vivo and rescues non-viable C.crescentus cells. However, we observe that the CtrA D51E and the unphosphorylated CtrA wild-type proteins have identical DNA affinities and produce identical DNase I protection footprints inside the C.crescentus replication origin. There fore, D51E promotes essential CtrA activities separate from increased DNA binding. Accordingly, we argue that CtrA protein recruitment to target DNA is not sufficient to regulate cell cycle progression.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=152873Documentos Relacionados
- A Dual Binding Site for Integration Host Factor and the Response Regulator CtrA inside the Caulobacter crescentus Replication Origin
- A Homolog of the CtrA Cell Cycle Regulator Is Present and Essential in Sinorhizobium meliloti
- The CtrA Response Regulator Mediates Temporal Control of Gene Expression during the Caulobacter Cell Cycle
- DNA methylation affects the cell cycle transcription of the CtrA global regulator in Caulobacter
- Conserved Response Regulator CtrA and IHF Binding Sites in the α-Proteobacteria Caulobacter crescentus and Rickettsia prowazekii Chromosomal Replication Origins