Roles of Pif1-like helicases in the maintenance of genomic stability
The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this family have been analyzed in some detail by in vitro and in vivo assays: the two baker's yeast helicases, ScPif1p and Rrm3p, the fission yeast Pfh1p and the human enzyme hPif1p. In vitro, these en...
| Main Authors: | , |
|---|---|
| Format: | Online |
| Language: | English |
| Published: |
Oxford University Press
2006
|
| Online Access: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616966/ |
| id |
pubmed-1616966 |
|---|---|
| recordtype |
oai_dc |
| spelling |
pubmed-16169662006-10-27 Roles of Pif1-like helicases in the maintenance of genomic stability Boulé, Jean-Baptiste Zakian, Virginia A. Survey and Summary The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this family have been analyzed in some detail by in vitro and in vivo assays: the two baker's yeast helicases, ScPif1p and Rrm3p, the fission yeast Pfh1p and the human enzyme hPif1p. In vitro, these enzymes are 5′ to 3′ DNA helicase and show little processivity. In vivo, ScPif1p, Rrm3p and probably Pfh1p, function in both the nucleus at specific genomic loci and in mitochondria, where they are needed for the stable maintenance of the genome as accessory helicases to the replication machinery. Interestingly, they act on common DNA substrates but appear to have largely non-overlapping cellular functions, ranging from Okazaki fragment processing, telomerase inhibition, to helping the replication fork progress through non-nucleosomal protein–DNA complexes. For example, both ScPif1p and Rrm3p affect the replication of telomeres, but in a different way: Pif1p inhibits telomerase-mediated telomere elongation by directly removing telomerase from a DNA end, whereas Rrm3p facilitates replication through telomeric DNA. Here we review the current knowledge on the Pif1-like helicases, as a first step towards understanding the basis of their functional specialization and mechanism of action. Oxford University Press 2006-09 2006-08-25 /pmc/articles/PMC1616966/ /pubmed/16935874 http://dx.doi.org/10.1093/nar/gkl561 Text en © 2006 The Author(s) |
| repository_type |
Open Access Journal |
| institution_category |
Foreign Institution |
| institution |
US National Center for Biotechnology Information |
| building |
NCBI PubMed |
| collection |
Online Access |
| language |
English |
| format |
Online |
| author |
Boulé, Jean-Baptiste Zakian, Virginia A. |
| spellingShingle |
Boulé, Jean-Baptiste Zakian, Virginia A. Roles of Pif1-like helicases in the maintenance of genomic stability |
| author_facet |
Boulé, Jean-Baptiste Zakian, Virginia A. |
| author_sort |
Boulé, Jean-Baptiste |
| title |
Roles of Pif1-like helicases in the maintenance of genomic stability |
| title_short |
Roles of Pif1-like helicases in the maintenance of genomic stability |
| title_full |
Roles of Pif1-like helicases in the maintenance of genomic stability |
| title_fullStr |
Roles of Pif1-like helicases in the maintenance of genomic stability |
| title_full_unstemmed |
Roles of Pif1-like helicases in the maintenance of genomic stability |
| title_sort |
roles of pif1-like helicases in the maintenance of genomic stability |
| description |
The Pif1p family of DNA helicases is conserved from yeast to humans. To date, four members of this family have been analyzed in some detail by in vitro and in vivo assays: the two baker's yeast helicases, ScPif1p and Rrm3p, the fission yeast Pfh1p and the human enzyme hPif1p. In vitro, these enzymes are 5′ to 3′ DNA helicase and show little processivity. In vivo, ScPif1p, Rrm3p and probably Pfh1p, function in both the nucleus at specific genomic loci and in mitochondria, where they are needed for the stable maintenance of the genome as accessory helicases to the replication machinery. Interestingly, they act on common DNA substrates but appear to have largely non-overlapping cellular functions, ranging from Okazaki fragment processing, telomerase inhibition, to helping the replication fork progress through non-nucleosomal protein–DNA complexes. For example, both ScPif1p and Rrm3p affect the replication of telomeres, but in a different way: Pif1p inhibits telomerase-mediated telomere elongation by directly removing telomerase from a DNA end, whereas Rrm3p facilitates replication through telomeric DNA. Here we review the current knowledge on the Pif1-like helicases, as a first step towards understanding the basis of their functional specialization and mechanism of action. |
| publisher |
Oxford University Press |
| publishDate |
2006 |
| url |
https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1616966/ |
| _version_ |
1611389987549347840 |