A conserved N-terminal motif in Rad54 is important for chromatin remodelling and homologous strand pairing

Journal of Biological Chemistry

Volumn 279, Issue 26, 2004, Pages 27824-27829

  Alexiadis, Vassilios ^a   Lusser, Alexandra ^a   Kadonaga, James T ^a  

^a SECTION OF MOLECULAR BIOLOGY   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOCHEMISTRY; CATALYSIS; DNA; ENZYME INHIBITION;

CHROMATIN; HOMOLOGOUS STRAND PAIRING;

PROTEINS;

ADENOSINE TRIPHOSPHATASE; DNA; RAD51 PROTEIN; RAD54 PROTEIN;

AMINO ACID SUBSTITUTION; AMINO TERMINAL SEQUENCE; ANIMAL CELL; ARTICLE; BASE PAIRING; CATALYSIS; CHROMATIN STRUCTURE; CONTROLLED STUDY; DNA STRAND; DROSOPHILA; ENZYME ACTIVITY; ENZYME INHIBITION; GENE MUTATION; HUMAN; HUMAN CELL; MOUSE; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN FUNCTION; PROTEIN MOTIF; SEQUENCE HOMOLOGY; STATISTICAL SIGNIFICANCE;

ADENOSINE TRIPHOSPHATASES; AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; CELL LINE; CHROMATIN; CONSERVED SEQUENCE; DNA; DNA, SINGLE-STRANDED; DNA-BINDING PROTEINS; DROSOPHILA PROTEINS; EGG PROTEINS; NUCLEIC ACID CONFORMATION; RAD51 RECOMBINASE; RECOMBINANT PROTEINS; RECOMBINATION, GENETIC; SEQUENCE DELETION; SPODOPTERA;

ANIMALIA; EUKARYOTA;

EID: 3042686376     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M402648200     Document Type: Article

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