A Dna Polymerase-alpha/ Primase Cofactor with Homology to Replication Protein A-32 Regulates Dna Replication in Mammalian Cells
نویسندگان
چکیده
HOMOLOGY TO REPLICATION PROTEIN A-32 REGULATES DNA REPLICATION IN MAMMALIAN CELLS Darren E. Casteel, Shunhui Zhuang, Ying Zeng, Fred W. Perrino*, Gerry R. Boss, Mehran Goulian, and Renate B. Pilz From the Department of Medicine and Cancer Center of the University of California, San Diego, La Jolla, CA 92093, and *the Department of Biochemistry and Cancer Center of Wake Forest University, Winston-Salem, NC 27157. Running Title: Accessory factor for DNA polymerase-alpha/primase Address correspondence to: Renate B. Pilz, Department of Medicine, University of California, San Diego, La Jolla, CA, 92093-0652; Tel: 858-534-8805; Fax: 858-534-1421; E-mail: [email protected]
منابع مشابه
An interaction between replication protein A and SV40 T antigen appears essential for primosome assembly during SV40 DNA replication.
Replication protein A from human cells (hRPA) is a multisubunit single-stranded DNA-binding protein (ssb) and is essential for SV40 DNA replication in vitro. The related RPA from Saccharomyces cerevisiae (scRPA) is unable to substitute for hRPA in SV40 DNA replication. To understand this species specificity, we evaluated human and yeast RPA in enzymatic assays with SV40 T antigen (TAg) and huma...
متن کاملAmino acids 257 to 288 of mouse p48 control the cooperation of polyomavirus large T antigen, replication protein A, and DNA polymerase alpha-primase to synthesize DNA in vitro.
Although p48 is the most conserved subunit of mammalian DNA polymerase alpha-primase (pol-prim), the polypeptide is the major species-specific factor for mouse polyomavirus (PyV) DNA replication. Human and murine p48 contain two regions (A and B) that show significantly lower homology than the rest of the protein. Chimerical human-murine p48 was prepared and coexpressed with three wild-type sub...
متن کاملThe mouse DNA polymerase alpha-primase subunit p48 mediates species-specific replication of polyomavirus DNA in vitro.
Mouse cell extracts support vigorous replication of polyomavirus (Py) DNA in vitro, while human cell extracts do not. However, the addition of purified mouse DNA polymerase alpha-primase to human cell extracts renders them permissive for Py DNA replication, suggesting that mouse polymerase alpha-primase determines the species specificity of Py DNA replication. We set out to identify the subunit...
متن کاملEvidence for participation of a multiprotein complex in yeast DNA replication in vitro.
Fractions containing a high molecular weight form (Mr approximately equal to 2 X 10(6] of the activity that replicates in vitro both the 2-micron yeast DNA plasmid and the chromosomal autonomously replicating sequence ars 1 can be prepared from cells of the budding yeast Saccharomyces. Protein complexes from the fractions associate in vitro with the replication origins of these DNA elements, as...
متن کاملReplication of simian virus 40 origin-containing DNA in vitro with purified proteins.
Simian virus 40 (SV40) DNA replication dependent on the SV40 origin of replication and the SV40 large tumor (T) antigen has been reconstituted in vitro with purified protein components isolated from HeLa cells. In addition to SV40 T antigen, these components included the DNA polymerase alpha-primase complex, topoisomerase I, and a fraction that contained a single-stranded DNA binding protein. T...
متن کامل