Linkage between phosphorylation of the origin recognition complex and its ATP binding activity in Saccharomyces cerevisiae

Journal of Biological Chemistry

Volumn 284, Issue 6, 2009, Pages 3396-3407

  Makise, Masaki ^a   Takehara, Masaya ^a   Kuniyasu, Akihiko ^a   Matsui, Nanako ^a   Nakayama, Hitoshi ^a   Mizushima, Tohru ^a,b  

^a KUMAMOTO UNIVERSITY   (Japan)

^b NONE   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ADENINE NUCLEOTIDE; ATP BINDING; CELL CYCLE; CYCLIN-DEPENDENT KINASE; DEPHOSPHORYLATION; DNA CONTENT; DNA REPLICATIONS; GENOME REPLICATION; IN-CELL; IN-VITRO; ORIGIN RECOGNITION COMPLEXES; S-PHASE; SACCHAROMYCES CEREVISIAE; YEAST STRAIN;

BINDING SITES; DNA; GENES; NUCLEIC ACIDS; PHASE TRANSITIONS; RANKINE CYCLE;

PHOSPHORYLATION;

ADENOSINE TRIPHOSPHATE; CHECKPOINT KINASE 2; ORIGIN RECOGNITION COMPLEX 2; ORIGIN RECOGNITION COMPLEX 6; SACCHAROMYCES CEREVISIAE PROTEIN; SERINE; UNCLASSIFIED DRUG; CELL CYCLE PROTEIN; CYCLIN DEPENDENT KINASE; FUNGAL DNA; ORIGIN RECOGNITION COMPLEX; PROTEIN SERINE THREONINE KINASE; RAD53 PROTEIN, S CEREVISIAE;

ARTICLE; CELL CYCLE G1 PHASE; CELL CYCLE M PHASE; CELL CYCLE PROGRESSION; CELL CYCLE REGULATION; CELL CYCLE S PHASE; CONTROLLED STUDY; DNA CONTENT; DNA REPLICATION; ENZYME BINDING; ENZYME PHOSPHORYLATION; FUNGAL CELL; FUNGAL STRAIN; MINICHROMOSOME; MUTATIONAL ANALYSIS; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEPHOSPHORYLATION; PROTEIN EXPRESSION; SITE DIRECTED MUTAGENESIS; CHROMOSOME; GENETICS; METABOLISM; PHOSPHORYLATION; PHYSIOLOGY; PROTEIN BINDING; SACCHAROMYCES CEREVISIAE;

SACCHAROMYCES CEREVISIAE;

ADENOSINE TRIPHOSPHATE; CELL CYCLE PROTEINS; CHROMOSOMES, FUNGAL; CYCLIN-DEPENDENT KINASES; DNA REPLICATION; DNA, FUNGAL; G1 PHASE; ORIGIN RECOGNITION COMPLEX; PHOSPHORYLATION; PROTEIN BINDING; PROTEIN-SERINE-THREONINE KINASES; S PHASE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 63649083216     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M804293200     Document Type: Article

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