Specific N-terminal interactions of the Escherichia coli SeqA protein are required to form multimers that restrain negative supercoils and form foci

Genes to Cells

Volumn 10, Issue 11, 2005, Pages 1039-1049

  Odsbu, Ingvild ^a   Klungsøyr, Hege K ^a   Fossum, Solveig ^a   Skarstad, Kirsten ^a  

^a INSTITUTE OF CANCER RESEARCH   (Norway)

Author keywords

[No Author keywords available]

Indexed keywords

ESCHERICHIA COLI PROTEIN; MUTANT PROTEIN; PLASMID DNA; POLYMER; SEQA PROTEIN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; BINDING AFFINITY; BINDING SITE; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; DIMERIZATION; DNA METHYLATION; DNA REPLICATION; DNA SUPERCOILING; ESCHERICHIA COLI; GENE INACTIVATION; IMMUNOFLUORESCENCE MICROSCOPY; IN VITRO STUDY; IN VIVO STUDY; NONHUMAN; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DNA INTERACTION; PROTEIN SYNTHESIS; WILD TYPE;

BACTERIAL OUTER MEMBRANE PROTEINS; DNA METHYLATION; DNA, SUPERHELICAL; DNA-BINDING PROTEINS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; NUCLEIC ACID CONFORMATION; PROTEIN BINDING; PROTEIN STRUCTURE, QUATERNARY; PROTEIN TRANSPORT; REPLICATION ORIGIN;

ESCHERICHIA COLI;

EID: 27644508886     PISSN: 13569597     EISSN: 13652443     Source Type: Journal    
DOI: 10.1111/j.1365-2443.2005.00898.x     Document Type: Article

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