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Strand Displacement Activity of PrimPol
Human PrimPol is a unique enzyme possessing DNA/RNA primase and DNA polymerase activities. In this work, we demonstrated that PrimPol efficiently fills a 5-nt gap and possesses the conditional strand displacement activity stimulated by Mn(2+) ions and accessory replicative proteins RPA and PolDIP2....
Autores principales: | , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
MDPI
2020
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7729601/ https://www.ncbi.nlm.nih.gov/pubmed/33261049 http://dx.doi.org/10.3390/ijms21239027 |
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author | Boldinova, Elizaveta O. Belousova, Ekaterina A. Gagarinskaya, Diana I. Maltseva, Ekaterina A. Khodyreva, Svetlana N. Lavrik, Olga I. Makarova, Alena V. |
author_facet | Boldinova, Elizaveta O. Belousova, Ekaterina A. Gagarinskaya, Diana I. Maltseva, Ekaterina A. Khodyreva, Svetlana N. Lavrik, Olga I. Makarova, Alena V. |
author_sort | Boldinova, Elizaveta O. |
collection | PubMed |
description | Human PrimPol is a unique enzyme possessing DNA/RNA primase and DNA polymerase activities. In this work, we demonstrated that PrimPol efficiently fills a 5-nt gap and possesses the conditional strand displacement activity stimulated by Mn(2+) ions and accessory replicative proteins RPA and PolDIP2. The DNA displacement activity of PrimPol was found to be more efficient than the RNA displacement activity and FEN1 processed the 5′-DNA flaps generated by PrimPol in vitro. |
format | Online Article Text |
id | pubmed-7729601 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2020 |
publisher | MDPI |
record_format | MEDLINE/PubMed |
spelling | pubmed-77296012020-12-12 Strand Displacement Activity of PrimPol Boldinova, Elizaveta O. Belousova, Ekaterina A. Gagarinskaya, Diana I. Maltseva, Ekaterina A. Khodyreva, Svetlana N. Lavrik, Olga I. Makarova, Alena V. Int J Mol Sci Article Human PrimPol is a unique enzyme possessing DNA/RNA primase and DNA polymerase activities. In this work, we demonstrated that PrimPol efficiently fills a 5-nt gap and possesses the conditional strand displacement activity stimulated by Mn(2+) ions and accessory replicative proteins RPA and PolDIP2. The DNA displacement activity of PrimPol was found to be more efficient than the RNA displacement activity and FEN1 processed the 5′-DNA flaps generated by PrimPol in vitro. MDPI 2020-11-27 /pmc/articles/PMC7729601/ /pubmed/33261049 http://dx.doi.org/10.3390/ijms21239027 Text en © 2020 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/). |
spellingShingle | Article Boldinova, Elizaveta O. Belousova, Ekaterina A. Gagarinskaya, Diana I. Maltseva, Ekaterina A. Khodyreva, Svetlana N. Lavrik, Olga I. Makarova, Alena V. Strand Displacement Activity of PrimPol |
title | Strand Displacement Activity of PrimPol |
title_full | Strand Displacement Activity of PrimPol |
title_fullStr | Strand Displacement Activity of PrimPol |
title_full_unstemmed | Strand Displacement Activity of PrimPol |
title_short | Strand Displacement Activity of PrimPol |
title_sort | strand displacement activity of primpol |
topic | Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7729601/ https://www.ncbi.nlm.nih.gov/pubmed/33261049 http://dx.doi.org/10.3390/ijms21239027 |
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