Structure and mutagenesis studies of the C-terminal region of licensing factor Cdt1 enable the identification of key residues for binding to replicative helicase Mcm proteins

Journal of Biological Chemistry

Volumn 285, Issue 21, 2010, Pages 15931-15940

  Jee, JunGoo ^a   Mizuno, Takeshi ^b,g   Kamada, Katsuhiko ^b,g   Tochio, Hidehito ^c   Chiba, Yasumasa ^d   Yanagi, Ken Ichiro ^b   Yasuda, Gentaro ^b   Hiroaki, Hidekazu ^e   Hanaoka, Fumio ^b,f   Shirakawa, Masahiro ^c  

^a TOKYO METROPOLITAN UNIVERSITY   (Japan)

^b Japan Science and Technology Agency   (Japan)

^c KYOTO UNIVERSITY   (Japan)

^d AJINOMOTO CO INC   (Japan)

^e KOBE UNIVERSITY GRADUATE SCHOOL OF MEDICINE   (Japan)

^f GAKUSHUIN UNIVERSITY   (Japan)

^g RIKEN   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

C-TERMINAL DOMAINS; C-TERMINAL FRAGMENTS; C-TERMINAL REGIONS; CELL DIVISIONS; DNA HELICASE; DNA REPLICATIONS; EVOLUTIONARY RELATIONSHIPS; HELICASES; IN-VITRO; LICENSING PROCESS; N-TERMINALS; SINGLE CELLS; SOLUTION STRUCTURES; STRUCTURE-BASED; YEAST VIABILITY;

BINDING ENERGY; CELL PROLIFERATION; DNA; GENES; MUTAGENESIS;

PROTEINS;

CELL CYCLE PROTEIN 6; HELICASE; MINICHROMOSOME MAINTENANCE PROTEIN; REPLICATION LICENSING FACTOR CDT1;

ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; DNA REPLICATION; IN VITRO STUDY; MOLECULAR EVOLUTION; MOLECULAR RECOGNITION; MUTAGENESIS; NONHUMAN; NUCLEAR MAGNETIC RESONANCE SPECTROSCOPY; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN DOMAIN; PROTEIN PROTEIN INTERACTION; PROTEIN STRUCTURE; SEQUENCE ALIGNMENT; STRUCTURAL HOMOLOGY; YEAST;

ANIMALS; CELL CYCLE PROTEINS; DNA HELICASES; DNA-BINDING PROTEINS; MADS DOMAIN PROTEINS; MICE; MUTAGENESIS; NUCLEAR MAGNETIC RESONANCE, BIOMOLECULAR; NUCLEAR PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; STRUCTURE-ACTIVITY RELATIONSHIP;

EUKARYOTA; SACCHAROMYCETALES;

EID: 77952415688     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M109.075333     Document Type: Article

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