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Structure–Function Studies of DNA Polymerase λ
[Image: see text] DNA polymerase λ (pol λ) functions in DNA repair with its main roles considered to be filling short gaps during repair of double-strand breaks by nonhomologous end joining and during base excision repair. As indicated by structural and biochemical studies over the past 10 years, po...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
American
Chemical Society
2014
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4018081/ https://www.ncbi.nlm.nih.gov/pubmed/24716527 http://dx.doi.org/10.1021/bi4017236 |
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author | Bebenek, Katarzyna Pedersen, Lars C. Kunkel, Thomas A. |
author_facet | Bebenek, Katarzyna Pedersen, Lars C. Kunkel, Thomas A. |
author_sort | Bebenek, Katarzyna |
collection | PubMed |
description | [Image: see text] DNA polymerase λ (pol λ) functions in DNA repair with its main roles considered to be filling short gaps during repair of double-strand breaks by nonhomologous end joining and during base excision repair. As indicated by structural and biochemical studies over the past 10 years, pol λ shares many common properties with other family X siblings (pol β, pol μ, and terminal deoxynucleotidyl transferase) but also has unique structural features that determine its specific functions. In this review, we consider how structural studies over the past decade furthered our understanding of the behavior and biological roles of pol λ. |
format | Online Article Text |
id | pubmed-4018081 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2014 |
publisher | American
Chemical Society |
record_format | MEDLINE/PubMed |
spelling | pubmed-40180812015-04-10 Structure–Function Studies of DNA Polymerase λ Bebenek, Katarzyna Pedersen, Lars C. Kunkel, Thomas A. Biochemistry [Image: see text] DNA polymerase λ (pol λ) functions in DNA repair with its main roles considered to be filling short gaps during repair of double-strand breaks by nonhomologous end joining and during base excision repair. As indicated by structural and biochemical studies over the past 10 years, pol λ shares many common properties with other family X siblings (pol β, pol μ, and terminal deoxynucleotidyl transferase) but also has unique structural features that determine its specific functions. In this review, we consider how structural studies over the past decade furthered our understanding of the behavior and biological roles of pol λ. American Chemical Society 2014-04-10 2014-05-06 /pmc/articles/PMC4018081/ /pubmed/24716527 http://dx.doi.org/10.1021/bi4017236 Text en Copyright © 2014 U.S. Government |
spellingShingle | Bebenek, Katarzyna Pedersen, Lars C. Kunkel, Thomas A. Structure–Function Studies of DNA Polymerase λ |
title | Structure–Function Studies of DNA Polymerase
λ |
title_full | Structure–Function Studies of DNA Polymerase
λ |
title_fullStr | Structure–Function Studies of DNA Polymerase
λ |
title_full_unstemmed | Structure–Function Studies of DNA Polymerase
λ |
title_short | Structure–Function Studies of DNA Polymerase
λ |
title_sort | structure–function studies of dna polymerase
λ |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4018081/ https://www.ncbi.nlm.nih.gov/pubmed/24716527 http://dx.doi.org/10.1021/bi4017236 |
work_keys_str_mv | AT bebenekkatarzyna structurefunctionstudiesofdnapolymerasel AT pedersenlarsc structurefunctionstudiesofdnapolymerasel AT kunkelthomasa structurefunctionstudiesofdnapolymerasel |