The linker sequence, joining the DNA-binding domain of the homologous transcription factors, Mlc and NagC, to the rest of the protein, determines the specificity of their DNA target recognition in Escherichia coli

Molecular Microbiology

Volumn 85, Issue 5, 2012, Pages 1007-1019

  Bréchemier Baey, Dominique ^a   Domínguez Ramírez, Lenin ^b,c   Plumbridge, Jacqueline ^a  

^a UNIVERSITÉ PARIS DESCARTES   (France)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c Metroipolitan Autonomous University Lerma   (Mexico)

Author keywords

[No Author keywords available]

Indexed keywords

ARGININE; MLC PROTEIN; NAGC PROTEIN; TRANSCRIPTION FACTOR; UNCLASSIFIED DRUG;

AMINO ACID SEQUENCE; AMINO ACID SUBSTITUTION; ARTICLE; BINDING SITE; CHIMERA; CONTROLLED STUDY; ESCHERICHIA COLI; GENE TARGETING; MOLECULAR MODEL; MOLECULAR RECOGNITION; NONHUMAN; NUCLEOTIDE SEQUENCE; PRIORITY JOURNAL; PROTEIN DNA BINDING; PROTEIN DOMAIN; PROTEIN MOTIF; PROTEIN STRUCTURE;

BINDING SITES; DNA, BACTERIAL; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HELIX-TURN-HELIX MOTIFS; PROTEIN BINDING; REPRESSOR PROTEINS;

ESCHERICHIA COLI;

EID: 84865554273     PISSN: 0950382X     EISSN: 13652958     Source Type: Journal    
DOI: 10.1111/j.1365-2958.2012.08158.x     Document Type: Article

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