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

Nucleic Acids Research

Volumn 31, Issue 6, 2003, Pages 1775-1779

  Siam, Rania ^a,b   Marczynski, Gregory T ^a  

^a MCGILL UNIVERSITY   (Canada)

^b SALK INSTITUTE FOR BIOLOGICAL STUDIES   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ASPARTIC ACID; BACTERIAL DNA; BACTERIAL PROTEIN; DEOXYRIBONUCLEASE I; GLUTAMIC ACID; PROTEIN CTRA; REGULATOR PROTEIN; UNCLASSIFIED DRUG;

BINDING AFFINITY; CAULOBACTER CRESCENTUS; CELL CYCLE; CELL VIABILITY; CONTROLLED STUDY; DNA FOOTPRINTING; DNA REPLICATION ORIGIN; GENE MUTATION; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN PHOSPHORYLATION; REGULATORY MECHANISM; REVIEW; WILD TYPE;

AMINO ACID SUBSTITUTION; BACTERIAL PROTEINS; BINDING SITES; BINDING, COMPETITIVE; CAULOBACTER CRESCENTUS; DNA, BACTERIAL; DNA-BINDING PROTEINS; ELECTROPHORETIC MOBILITY SHIFT ASSAY; GENOTYPE; GLUTAMIC ACID; KINETICS; PHOSPHORYLATION; PROTEIN BINDING; REPLICATION ORIGIN; TRANSCRIPTION FACTORS;

BACTERIA (MICROORGANISMS); CAULOBACTER VIBRIOIDES; NEGIBACTERIA;

EID: 0037443967     PISSN: 03051048     EISSN: None     Source Type: Journal    
DOI: 10.1093/nar/gkg271     Document Type: Review

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