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Thermococcus kodakarensis encodes three MCM homologs but only one is essential
The minichromosome maintenance (MCM) complex is thought to function as the replicative helicase in archaea and eukaryotes. In eukaryotes, this complex is an assembly of six different but related polypeptides (MCM2-7) but, in most archaea, one MCM protein assembles to form a homohexameric complex. At...
Autores principales: | , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
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Oxford University Press
2011
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3239210/ https://www.ncbi.nlm.nih.gov/pubmed/21821658 http://dx.doi.org/10.1093/nar/gkr624 |
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author | Pan, Miao Santangelo, Thomas J. Li, Zhuo Reeve, John N. Kelman, Zvi |
author_facet | Pan, Miao Santangelo, Thomas J. Li, Zhuo Reeve, John N. Kelman, Zvi |
author_sort | Pan, Miao |
collection | PubMed |
description | The minichromosome maintenance (MCM) complex is thought to function as the replicative helicase in archaea and eukaryotes. In eukaryotes, this complex is an assembly of six different but related polypeptides (MCM2-7) but, in most archaea, one MCM protein assembles to form a homohexameric complex. Atypically, the Thermococcus kodakarensis genome encodes three archaeal MCM homologs, here designated MCM1-3, although MCM1 and MCM2 are unusual in having long and unique N-terminal extensions. The results reported establish that MCM2 and MCM3 assemble into homohexamers and exhibit DNA binding, helicase and ATPase activities in vitro typical of archaeal MCMs. In contrast, MCM1 does not form homohexamers and although MCM1 binds DNA and has ATPase activity, it has only minimal helicase activity in vitro. Removal of the N-terminal extension had no detectable effects on MCM1 but increased the helicase activity of MCM2. A T. kodakarensis strain with the genes TK0096 (MCM1) and TK1361 (MCM2) deleted has been constructed that exhibits no detectable defects in growth or viability, but all attempts to delete TK1620 (MCM3) have been unsuccessful arguing that that MCM3 is essential and is likely the replicative helicase in T. kodakarensis. The origins and possible function(s) of the three MCM proteins are discussed. |
format | Online Article Text |
id | pubmed-3239210 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2011 |
publisher | Oxford University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-32392102011-12-16 Thermococcus kodakarensis encodes three MCM homologs but only one is essential Pan, Miao Santangelo, Thomas J. Li, Zhuo Reeve, John N. Kelman, Zvi Nucleic Acids Res Nucleic Acid Enzymes The minichromosome maintenance (MCM) complex is thought to function as the replicative helicase in archaea and eukaryotes. In eukaryotes, this complex is an assembly of six different but related polypeptides (MCM2-7) but, in most archaea, one MCM protein assembles to form a homohexameric complex. Atypically, the Thermococcus kodakarensis genome encodes three archaeal MCM homologs, here designated MCM1-3, although MCM1 and MCM2 are unusual in having long and unique N-terminal extensions. The results reported establish that MCM2 and MCM3 assemble into homohexamers and exhibit DNA binding, helicase and ATPase activities in vitro typical of archaeal MCMs. In contrast, MCM1 does not form homohexamers and although MCM1 binds DNA and has ATPase activity, it has only minimal helicase activity in vitro. Removal of the N-terminal extension had no detectable effects on MCM1 but increased the helicase activity of MCM2. A T. kodakarensis strain with the genes TK0096 (MCM1) and TK1361 (MCM2) deleted has been constructed that exhibits no detectable defects in growth or viability, but all attempts to delete TK1620 (MCM3) have been unsuccessful arguing that that MCM3 is essential and is likely the replicative helicase in T. kodakarensis. The origins and possible function(s) of the three MCM proteins are discussed. Oxford University Press 2011-12 2011-08-05 /pmc/articles/PMC3239210/ /pubmed/21821658 http://dx.doi.org/10.1093/nar/gkr624 Text en © The Author(s) 2011. Published by Oxford University Press. http://creativecommons.org/licenses/by-nc/3.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/3.0), which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Nucleic Acid Enzymes Pan, Miao Santangelo, Thomas J. Li, Zhuo Reeve, John N. Kelman, Zvi Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title | Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title_full | Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title_fullStr | Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title_full_unstemmed | Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title_short | Thermococcus kodakarensis encodes three MCM homologs but only one is essential |
title_sort | thermococcus kodakarensis encodes three mcm homologs but only one is essential |
topic | Nucleic Acid Enzymes |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3239210/ https://www.ncbi.nlm.nih.gov/pubmed/21821658 http://dx.doi.org/10.1093/nar/gkr624 |
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