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The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions
DNA polymerase _ (pol _) holds a special position among the growing family of eukaryotic DNA polymerases. In fact, pol _ is associated with DNA primase to form a four subunit complex and, as a consequence, is the only enzyme able to start DNA synthesis de novo. Because of this peculiarity the major...
Autores principales: | , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
TheScientificWorldJOURNAL
2003
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5974749/ https://www.ncbi.nlm.nih.gov/pubmed/12806117 http://dx.doi.org/10.1100/tsw.2003.05 |
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author | Muzi-Falconi, Marco Giannattasio, Michele Foiani, Marco Plevani, Paolo |
author_facet | Muzi-Falconi, Marco Giannattasio, Michele Foiani, Marco Plevani, Paolo |
author_sort | Muzi-Falconi, Marco |
collection | PubMed |
description | DNA polymerase _ (pol _) holds a special position among the growing family of eukaryotic DNA polymerases. In fact, pol _ is associated with DNA primase to form a four subunit complex and, as a consequence, is the only enzyme able to start DNA synthesis de novo. Because of this peculiarity the major role of the DNA polymerase _-primase complex (pol-prim) is in the initiation of DNA replication at chromosomal origins and in the discontinuous synthesis of Okazaki fragments on the lagging strand of the replication fork. However, pol-prim seems to play additional roles in other complex cellular processes, such as the response to DNA damage, telomere maintenance, and the epigenetic control of higher order chromatin assembly. |
format | Online Article Text |
id | pubmed-5974749 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2003 |
publisher | TheScientificWorldJOURNAL |
record_format | MEDLINE/PubMed |
spelling | pubmed-59747492018-06-10 The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions Muzi-Falconi, Marco Giannattasio, Michele Foiani, Marco Plevani, Paolo ScientificWorldJournal Mini-Review Article DNA polymerase _ (pol _) holds a special position among the growing family of eukaryotic DNA polymerases. In fact, pol _ is associated with DNA primase to form a four subunit complex and, as a consequence, is the only enzyme able to start DNA synthesis de novo. Because of this peculiarity the major role of the DNA polymerase _-primase complex (pol-prim) is in the initiation of DNA replication at chromosomal origins and in the discontinuous synthesis of Okazaki fragments on the lagging strand of the replication fork. However, pol-prim seems to play additional roles in other complex cellular processes, such as the response to DNA damage, telomere maintenance, and the epigenetic control of higher order chromatin assembly. TheScientificWorldJOURNAL 2003-03-17 /pmc/articles/PMC5974749/ /pubmed/12806117 http://dx.doi.org/10.1100/tsw.2003.05 Text en Copyright © 2003 Marco Muzi-Falconi et al. https://creativecommons.org/licenses/by/3.0/ This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Mini-Review Article Muzi-Falconi, Marco Giannattasio, Michele Foiani, Marco Plevani, Paolo The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title | The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title_full | The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title_fullStr | The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title_full_unstemmed | The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title_short | The DNA Polymerase ʱ-Primase Complex: Multiple Functions and Interactions |
title_sort | dna polymerase ʱ-primase complex: multiple functions and interactions |
topic | Mini-Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5974749/ https://www.ncbi.nlm.nih.gov/pubmed/12806117 http://dx.doi.org/10.1100/tsw.2003.05 |
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