The MPH1 gene of Saccharomyces cerevisiae functions in Okazaki fragment processing

Journal of Biological Chemistry

Volumn 284, Issue 16, 2009, Pages 10376-10386

  Kang, Young Hoon ^a   Kang, Min Jung ^a   Kim, Jeong Hoon ^a   Lee, Chul Hwan ^a   Cho, Il Taeg ^a   Hurwitz, Jerard ^b   Seo, Yeon Soo ^a  

^a Korea Advanced Institute of Science and Technology (KAIST)   (South Korea)

^b MEMORIAL SLOAN KETTERING CANCER CENTER   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

ATP HYDROLYSIS; DNA HELICASE; DNA SUBSTRATES; DUPLEX STRUCTURES; ENDONUCLEASE ACTIVITIES; EXONUCLEASE ACTIVITY; GENETIC DATA; HELICASE; HELICASE ACTIVITIES; IN-CELL; IN-VIVO; INHIBITORY EFFECT; MUTANT PROTEINS; N-TERMINAL; OKAZAKI FRAGMENTS; REPLICATION PROTEIN A; SACCHAROMYCES CEREVISIAE; STIMULATORY EFFECTS; STRUCTURED SUBSTRATE; TEMPERATURE-SENSITIVE GROWTH;

AMINES; AMINO ACIDS; DNA; GENE ENCODING; NUCLEIC ACIDS; ORGANIC ACIDS;

SUBSTRATES;

ADENOSINE TRIPHOSPHATE; DNA2 ENDONUCLEASE; ENDONUCLEASE; EXONUCLEASE; FLAP ENDONUCLEASE 1; FUNGAL PROTEIN; HELICASE; MUTATOR PHENOTYPE 1 PROTEIN; OKAZAKI FRAGMENT; UNCLASSIFIED DRUG; ACYLTRANSFERASE; DEAD BOX PROTEIN; DNA; DNA2 PROTEIN, S CEREVISIAE; FEN1 PROTEIN, S CEREVISIAE; MEMBRANE PROTEIN; MPH1 PROTEIN, S CEREVISIAE; OKAZAKI FRAGMENTS; SACCHAROMYCES CEREVISIAE PROTEIN;

ARTICLE; CONTROLLED STUDY; DNA METABOLISM; DNA NICK TRANSLATION; ENZYME ACTIVATION; FUNGUS GROWTH; HYDROLYSIS; LETHAL MUTANT; NONHUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEIN FUNCTION; PROTEIN PURIFICATION; SACCHAROMYCES CEREVISIAE; TEMPERATURE SENSITIVITY; DNA REPLICATION; GENETICS; METABOLISM; MOLECULAR GENETICS; MUTATION; NUCLEOTIDE SEQUENCE; PHENOTYPE;

SACCHAROMYCES CEREVISIAE;

ACETYLTRANSFERASES; ADENOSINE TRIPHOSPHATE; BASE SEQUENCE; DEAD-BOX RNA HELICASES; DNA; DNA HELICASES; DNA REPLICATION; ENZYME ACTIVATION; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA; MUTATION; PHENOTYPE; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS;

EID: 67449091971     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M808894200     Document Type: Article

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