Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases

To cleave DNA, the Type III RM (restriction–modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocati...

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Autor principal: Szczelkun, Mark D.
Formato: Texto
Lenguaje:English
Publicado: Portland Press Ltd. 2011
Materias:
Independent Meetings
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064402/
https://www.ncbi.nlm.nih.gov/pubmed/21428945
http://dx.doi.org/10.1042/BST0390589
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author Szczelkun, Mark D.
author_facet Szczelkun, Mark D.
author_sort Szczelkun, Mark D.
collection PubMed
description To cleave DNA, the Type III RM (restriction–modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches.
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spelling pubmed-30644022011-03-29 Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases Szczelkun, Mark D. Biochem Soc Trans Independent Meetings To cleave DNA, the Type III RM (restriction–modification) enzymes must communicate the relative orientation of two recognition sequences, which may be separated by many thousands of base pairs. This long-range interaction requires ATP hydrolysis by a helicase domain, and both active (DNA translocation) and passive (DNA sliding) modes of motion along DNA have been proposed. Potential roles for ATP binding and hydrolysis by the helicase domains are discussed, with a focus on bipartite ATPases that act as molecular switches. Portland Press Ltd. 2011-03-22 2011-04-01 /pmc/articles/PMC3064402/ /pubmed/21428945 http://dx.doi.org/10.1042/BST0390589 Text en © 2011 The Author(s) The author(s) has paid for this article to be freely available under the terms of the Creative Commons Attribution Non-Commercial Licence (http://creativecommons.org/licenses/by-nc/2.5/) which permits unrestricted non-commercial use, distribution and reproduction in any medium, provided the original work is properly cited. http://creativecommons.org/licenses/by-nc/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.
spellingShingle Independent Meetings
Szczelkun, Mark D.
Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title_full Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title_fullStr Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title_full_unstemmed Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title_short Translocation, switching and gating: potential roles for ATP in long-range communication on DNA by Type III restriction endonucleases
title_sort translocation, switching and gating: potential roles for atp in long-range communication on dna by type iii restriction endonucleases
topic Independent Meetings
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC3064402/
https://www.ncbi.nlm.nih.gov/pubmed/21428945
http://dx.doi.org/10.1042/BST0390589
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