Spt16 and Pob3 of Saccharomyces cerevisiae form an essential, abundant heterodimer that is nuclear, chromatin-associated, and copurifies with DNA polymerase α

Biochemistry

Volumn 38, Issue 28, 1999, Pages 8961-8971

  Wittmeyer, Jacqueline ^a   Joss, Lisa ^a   Formosa, Tim ^a  

^a UNIVERSITY OF UTAH SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DNA DIRECTED DNA POLYMERASE ALPHA; FUNGAL PROTEIN; PROTEIN POB3; PROTEIN SPT16; UNCLASSIFIED DRUG;

ARTICLE; CHROMATIN; ENZYME SUBUNIT; NONHUMAN; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STABILITY; SACCHAROMYCES CEREVISIAE;

ACETYLTRANSFERASES; ADENOSINE TRIPHOSPHATASES; CARRIER PROTEINS; CELL CYCLE PROTEINS; CHROMATIN; CHROMATOGRAPHY, AFFINITY; CHROMATOGRAPHY, GEL; CHROMATOGRAPHY, ION EXCHANGE; DIMERIZATION; DNA POLYMERASE I; DURAPATITE; ENZYME ACTIVATION; FUNGAL PROTEINS; HISTONE ACETYLTRANSFERASES; IMMUNOBLOTTING; MACROMOLECULAR SUBSTANCES; NUCLEAR PROTEINS; PEPTIDE CHAIN ELONGATION, TRANSLATIONAL; SACCHAROMYCES CEREVISIAE; SACCHAROMYCES CEREVISIAE PROTEINS; TRANSCRIPTION FACTORS;

EID: 0033551430     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi982851d     Document Type: Article

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