σ54-dependent transcription activator phage shock protein F of Escherichia coli: A fragmentation approach to identify sequences that contribute to self-association

Biochemical Journal

Volumn 378, Issue 3, 2004, Pages 735-744

  Bordes, Patricia ^a   Wigneshweraraj, Siva R ^a   Zhang, Xiaodong ^a   Buck, Martin ^a  

^a IMPERIAL COLLEGE LONDON   (United Kingdom)

Author keywords

54; AAA protein; FeBABE; Oligomerization; Transcription activator

Indexed keywords

CELLS; CROSSLINKING; ESCHERICHIA COLI; HYDROLYSIS; MOLECULAR STRUCTURE; OLIGOMERS;

CELLULAR FUNCTIONS; NUCLEOTIDES;

PROTEINS;

BACTERIAL PROTEIN; RNA POLYMERASE; TRANSCRIPTION ACTIVATOR PHAGE SHOCK PROTEIN F; UNCLASSIFIED DRUG; ADENOSINE TRIPHOSPHATE; DNA; DNA BINDING PROTEIN; DNA DIRECTED RNA POLYMERASE; ESCHERICHIA COLI PROTEIN; HYBRID PROTEIN; NUCLEOTIDE; PEPTIDE FRAGMENT; PSPF PROTEIN, E COLI; RPON PROTEIN, E COLI; SIGMA FACTOR; SIGMA FACTOR RPON; TRANSACTIVATOR PROTEIN;

ARTICLE; CELL FUNCTION; CROSS LINKING; DNA FOOTPRINTING; ESCHERICHIA COLI; FRAGMENTATION REACTION; HYDROLYSIS; NONHUMAN; PRIORITY JOURNAL; PROMOTER REGION; PROTEIN ASSEMBLY; PROTEIN BINDING; PROTEIN INTERACTION; TRANSCRIPTION INITIATION; AMINO ACID SEQUENCE; BINDING SITE; CHEMISTRY; GENE EXPRESSION REGULATION; GENETIC TRANSCRIPTION; GENETICS; ISOLATION AND PURIFICATION; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PROTEIN MOTIF; PROTEIN TERTIARY STRUCTURE; SEQUENCE ANALYSIS;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; NEGIBACTERIA;

ADENOSINE TRIPHOSPHATE; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; BASE SEQUENCE; BINDING SITES; DNA; DNA-BINDING PROTEINS; DNA-DIRECTED RNA POLYMERASES; ESCHERICHIA COLI PROTEINS; GENE EXPRESSION REGULATION; MOLECULAR SEQUENCE DATA; MUTATION; NUCLEOTIDES; PEPTIDE FRAGMENTS; PROMOTER REGIONS (GENETICS); PROTEIN STRUCTURE, TERTIARY; RECOMBINANT FUSION PROTEINS; RNA POLYMERASE SIGMA 54; SEQUENCE ANALYSIS, PROTEIN; SIGMA FACTOR; TRANS-ACTIVATORS; TRANSCRIPTION, GENETIC;

EID: 1642423500     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031464     Document Type: Article

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