Maturation of bacteriophage T4 lagging strand fragments depends on interaction of T4 RNase H with T4 32 protein rather than the T4 gene 45 clamp

Journal of Biological Chemistry

Volumn 280, Issue 13, 2005, Pages 12876-12887

  Gangisetty, Omkaram ^a,b   Jones, Charles E ^a   Bhagwat, Medha ^a,c   Nossal, Nancy G ^a  

^a NATIONAL INSTITUTE OF DIABETES AND DIGESTIVE AND KIDNEY DISEASES   (United States)

^b ROSWELL PARK CANCER INSTITUTE   (United States)

^c NATIONAL INSTITUTES OF HEALTH   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CATALYSIS; CRYSTAL STRUCTURE; DNA; ENZYMES; GENES; PROTEINS; RNA; SUBSTRATES;

EXONUCLEASE ACTIVITY; NUCLEASE FAMILY; RNA PRIMERS; STRAND FRAGMENTS;

BACTERIOPHAGES;

DNA; RIBONUCLEASE;

AMINO TERMINAL SEQUENCE; ARTICLE; BACTERIOPHAGE T4; CARBOXY TERMINAL SEQUENCE; CLAMP; CRYSTAL STRUCTURE; DNA REPLICATION; DNA STRAND; DNA SYNTHESIS; ENZYME ACTIVE SITE; ENZYME ACTIVITY; ENZYME SUBSTRATE; GENE DELETION; GENE REPLICATION; MOLECULAR INTERACTION; PRIORITY JOURNAL; PROTEIN DNA INTERACTION; PROTEIN LOCALIZATION; PROTEIN MOTIF;

AMINO ACID SEQUENCE; BACTERIOPHAGE T4; BINDING SITES; CATALYTIC DOMAIN; CRYSTALLOGRAPHY, X-RAY; DNA; DNA PRIMERS; GENE DELETION; GENETIC COMPLEMENTATION TEST; HUMANS; MODELS, GENETIC; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; MUTATION; PLASMIDS; POINT MUTATION; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN STRUCTURE, TERTIARY; RIBONUCLEASES; RNA; SEPHAROSE;

EID: 16844381984     PISSN: 00219258     EISSN: None     Source Type: Journal    
DOI: 10.1074/jbc.M414025200     Document Type: Article

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