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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Boss, Gerry R. Pilz, Renate B. Zeng, Ying Goulian, Mehran Casteel, Darren E. Perrino, Fred W. Zhuang, Shunhui |
| Description | Author Affiliation: Casteel DE ( Department of Medicine and Cancer Center of the University of California, San Diego, La Jolla, California 92093, USA.) |
| Abstract | alpha-Accessory factor (AAF) stimulates the activity of DNA polymerase-alpha.primase, the only enzyme known to initiate DNA replication in eukaryotic cells ( Goulian, M., Heard, C. J., and Grimm, S. L. (1990) J. Biol. Chem. 265, 13221-13230 ). We purified the AAF heterodimer composed of 44- and 132-kDa subunits from cultured cells and identified full-length cDNA clones using amino acid sequences from internal peptides. AAF-132 demonstrated no homologies to known proteins; AAF-44, however, is evolutionarily related to the 32-kDa subunit of replication protein A (RPA-32) and contains an oligonucleotide/oligosaccharide-binding (OB) fold domain similar to the OB fold domains of RPA involved in single-stranded DNA binding. Epitope-tagged versions of AAF-44 and -132 formed a complex in intact cells, and purified recombinant AAF-44 bound to single-stranded DNA and stimulated DNA primase activity only in the presence of AAF-132. Mutations in conserved residues within the OB fold of AAF-44 reduced DNA binding activity of the AAF-44.AAF-132 complex. Immunofluorescence staining of AAF-44 and AAF-132 in S phase-enriched HeLa cells demonstrated punctate nuclear staining, and AAF co-localized with proliferating cell nuclear antigen, a marker for replication foci containing DNA polymerase-alpha.primase and RPA. Small interfering RNA-mediated depletion of AAF-44 in tumor cell lines inhibited [methyl-(3)H]thymidine uptake into DNA but did not affect cell viability. We conclude that AAF shares structural and functional similarities with RPA-32 and regulates DNA replication, consistent with its ability to increase polymerase-alpha.primase template affinity and stimulate both DNA primase and polymerase-alpha activities in vitro. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 9 |
| Volume Number | 284 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2009-02-27 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | DNA Polymerase I Metabolism DNA Primase DNA Replication Proteins Replication Protein A Amino Acid Sequence Animals Blotting, Northern Cells, Cultured Genetics Fluorescent Antibody Technique HeLa Cells Immunoprecipitation Kidney Cytology Leukemia L1210 Pathology Mice Molecular Sequence Data Mutagenesis, Site-Directed Phylogeny Protein Biosynthesis Protein Multimerization Antagonists & Inhibitors RNA, Messenger RNA, Small Interfering Pharmacology Reverse Transcriptase Polymerase Chain Reaction Sequence Homology, Amino Acid Transcription, Genetic Transfection Research Support, N.I.H., Extramural Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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