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The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain

Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B-domains of the archaeo-eukaryotic GINS proteins i...

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Detalles Bibliográficos
Autores principales: Swiatek, Agnieszka, MacNeill, Stuart A
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2010
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2861644/
https://www.ncbi.nlm.nih.gov/pubmed/20385010
http://dx.doi.org/10.1186/1745-6150-5-17
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author Swiatek, Agnieszka
MacNeill, Stuart A
author_facet Swiatek, Agnieszka
MacNeill, Stuart A
author_sort Swiatek, Agnieszka
collection PubMed
description Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B-domains of the archaeo-eukaryotic GINS proteins in the form of a conserved structural domain comprising a three-stranded antiparallel β-sheet adjacent to an α-helix and a two-stranded β-sheet or hairpin. The presence of a shared domain in archaeal PriS and GINS proteins, the genes for which are often found adjacent on the chromosome, suggests simple mechanisms for the evolution of these proteins. REVIEWERS: This article was reviewed by Zvi Kelman (nominated by Michael Galperin) and Kira Makarova.
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spelling pubmed-28616442010-04-30 The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain Swiatek, Agnieszka MacNeill, Stuart A Biol Direct Discovery notes Primase and GINS are essential factors for chromosomal DNA replication in eukaryotic and archaeal cells. Here we describe a previously undetected relationship between the C-terminal domain of the catalytic subunit (PriS) of archaeal primase and the B-domains of the archaeo-eukaryotic GINS proteins in the form of a conserved structural domain comprising a three-stranded antiparallel β-sheet adjacent to an α-helix and a two-stranded β-sheet or hairpin. The presence of a shared domain in archaeal PriS and GINS proteins, the genes for which are often found adjacent on the chromosome, suggests simple mechanisms for the evolution of these proteins. REVIEWERS: This article was reviewed by Zvi Kelman (nominated by Michael Galperin) and Kira Makarova. BioMed Central 2010-04-12 /pmc/articles/PMC2861644/ /pubmed/20385010 http://dx.doi.org/10.1186/1745-6150-5-17 Text en Copyright ©2010 Swiatek and MacNeill; licensee BioMed Central Ltd. http://creativecommons.org/licenses/by/2.0 This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/2.0), which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Discovery notes
Swiatek, Agnieszka
MacNeill, Stuart A
The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title_full The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title_fullStr The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title_full_unstemmed The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title_short The archaeo-eukaryotic GINS proteins and the archaeal primase catalytic subunit PriS share a common domain
title_sort archaeo-eukaryotic gins proteins and the archaeal primase catalytic subunit pris share a common domain
topic Discovery notes
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2861644/
https://www.ncbi.nlm.nih.gov/pubmed/20385010
http://dx.doi.org/10.1186/1745-6150-5-17
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