Glutamate at the phosphorylation site of response regulator CtrA provides essential activities without increasing DNA binding

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...

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Bibliographic Details
Published in:Nucleic acids research 2003-03, Vol.31 (6), p.1775-1779
Main Authors: Siam, Rania, Marczynski, Gregory T.
Format: Article
Language:English
Subjects:
Amino Acid Substitution
Bacterial Proteins
Binding Sites - genetics
Binding, Competitive
Caulobacter crescentus - genetics
Caulobacter crescentus - metabolism
DNA, Bacterial - genetics
DNA, Bacterial - metabolism
DNA-Binding Proteins - genetics
DNA-Binding Proteins - metabolism
Electrophoretic Mobility Shift Assay
Genotype
Glutamic Acid - genetics
Kinetics
Phosphorylation
Protein Binding
Replication Origin - genetics
Transcription Factors - genetics
Transcription Factors - metabolism
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Summary: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.
ISSN:0305-1048
1362-4962
1362-4962
DOI:10.1093/nar/gkg271