The yeast DNA polymerase-primase complex: Genes and proteins
| Autor: | Plevani, P., Foiani, M., Muzi Falconi, M, Pizzagalli, A., Santocanale, C., Francesconi, S., Valsasnini, P., Comedini, A., Piatti, S., Lucchini, G., Falconi, M.Muzi |
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| Přispěvatelé: | Università degli Studi di Milano [Milano] (UNIMI) |
| Rok vydání: | 1988 |
| Předmět: |
DNA polymerase
[SDV]Life Sciences [q-bio] MESH: RNA Nucleotidyltransferases MESH: DNA Replication MESH: Amino Acid Sequence DNA-Directed DNA Polymerase Biochemistry DNA polymerase delta MESH: Structure-Activity Relationship Structural Biology MESH: DNA-Directed DNA Polymerase Polymerase Immunoassay Genetics 0303 health sciences DNA clamp biology 030302 biochemistry & molecular biology RNA Nucleotidyltransferases MESH: Saccharomyces cerevisiae MESH: DNA Primase Electrophoresis Polyacrylamide Gel Primase MESH: Immunoassay DNA Replication MESH: Mutation DNA polymerase II Biophysics DNA Primase Saccharomyces cerevisiae MESH: Sequence Homology Nucleic Acid Structure-Activity Relationship 03 medical and health sciences Sequence Homology Nucleic Acid MESH: DNA Polymerase II Humans Amino Acid Sequence MESH: DNA Polymerase I 030304 developmental biology MESH: Humans Binding Sites DNA replication DNA Polymerase II DNA Polymerase I MESH: Binding Sites Mutation biology.protein DNA polymerase I MESH: Electrophoresis Polyacrylamide Gel |
| Zdroj: | Biomedica Biochimica Acta Biomedica Biochimica Acta, Akademie Verlag, 1988, 951 (2-3), pp.268-273. ⟨10.1016/0167-4781(88)90096-6⟩ Scopus-Elsevier |
| ISSN: | 0167-4781 0232-766X |
| DOI: | 10.1016/0167-4781(88)90096-6 |
| Popis: | International audience; The yeast DNA polymerase-primase complex is composed of four polypeptides designated p180, p74, p58 and p48. All the genes coding for these polypeptides have now been cloned. By protein sequence comparison we found that yeast DNA polymerase I (alpha) shares three major regions of homology with several DNA polymerases. A fourth region, called region P, is conserved in yeast and human DNA polymerase alpha. The site of a temperature-sensitive mutation in the POL1 gene which causes decreased stability of the polymerase-primase complex has been sequenced and falls in this region. We hypothesize that region P is important for protein-protein interactions. Highly selective biochemical methods might be similarly important to distinguish functional domains in the polymerase-primase complex. An autocatalytic affinity labeling procedure has been applied to map the active center of yeast DNA primase. From this approach we conclude that both primase subunits (p48 and p58) participate in the formation of the catalytic site of the enzyme. |
| Databáze: | OpenAIRE |
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