Archaeal MCM has separable processivity, substrate choice and helicase domains

The mini-chromosome maintenance (MCM) complex is the principal candidate for the replicative helicase of archaea and eukaryotes. Here, we describe a functional dissection of the roles of the three principal structural modules of the homomultimeric MCM of the hyperthermophilic archaeon Sulfolobus sol...

Full description

Bibliographic Details
Main Authors:	Barry, Elizabeth R., McGeoch, Adam T., Kelman, Zvi, Bell, Stephen D.
Format:	Online
Language:	English
Published:	Oxford University Press 2007
Online Access:	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807962/

id	pubmed-1807962
recordtype	oai_dc
spelling	pubmed-18079622007-03-02 Archaeal MCM has separable processivity, substrate choice and helicase domains Barry, Elizabeth R. McGeoch, Adam T. Kelman, Zvi Bell, Stephen D. Nucleic Acid Enzymes The mini-chromosome maintenance (MCM) complex is the principal candidate for the replicative helicase of archaea and eukaryotes. Here, we describe a functional dissection of the roles of the three principal structural modules of the homomultimeric MCM of the hyperthermophilic archaeon Sulfolobus solfataricus. Our results include the first analysis of the central AAA+ domain in isolation. This domain possesses ATPase and helicase activity, defining this as the minimal helicase domain. Reconstitution experiments show that the helicase activity of the AAA+ domain can be stimulated by addition of the isolated N-terminal half in trans. Addition of the N-terminus influences both the processivity of the helicase and the choice of substrate that can be melted by the ATPase domain. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. These results provide the first evidence for extensive regulatory inter-domain communication within the MCM complex. Oxford University Press 2007-02 2007-01-26 /pmc/articles/PMC1807962/ /pubmed/17259218 http://dx.doi.org/10.1093/nar/gkl1117 Text en © 2007 The Author(s). This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.
repository_type	Open Access Journal
institution_category	Foreign Institution
institution	US National Center for Biotechnology Information
building	NCBI PubMed
collection	Online Access
language	English
format	Online
author	Barry, Elizabeth R. McGeoch, Adam T. Kelman, Zvi Bell, Stephen D.
spellingShingle	Barry, Elizabeth R. McGeoch, Adam T. Kelman, Zvi Bell, Stephen D. Archaeal MCM has separable processivity, substrate choice and helicase domains
author_facet	Barry, Elizabeth R. McGeoch, Adam T. Kelman, Zvi Bell, Stephen D.
author_sort	Barry, Elizabeth R.
title	Archaeal MCM has separable processivity, substrate choice and helicase domains
title_short	Archaeal MCM has separable processivity, substrate choice and helicase domains
title_full	Archaeal MCM has separable processivity, substrate choice and helicase domains
title_fullStr	Archaeal MCM has separable processivity, substrate choice and helicase domains
title_full_unstemmed	Archaeal MCM has separable processivity, substrate choice and helicase domains
title_sort	archaeal mcm has separable processivity, substrate choice and helicase domains
description	The mini-chromosome maintenance (MCM) complex is the principal candidate for the replicative helicase of archaea and eukaryotes. Here, we describe a functional dissection of the roles of the three principal structural modules of the homomultimeric MCM of the hyperthermophilic archaeon Sulfolobus solfataricus. Our results include the first analysis of the central AAA+ domain in isolation. This domain possesses ATPase and helicase activity, defining this as the minimal helicase domain. Reconstitution experiments show that the helicase activity of the AAA+ domain can be stimulated by addition of the isolated N-terminal half in trans. Addition of the N-terminus influences both the processivity of the helicase and the choice of substrate that can be melted by the ATPase domain. The degenerate helix-turn-helix domain at the C-terminus of MCM exerts a negative effect on the helicase activity of the complex. These results provide the first evidence for extensive regulatory inter-domain communication within the MCM complex.
publisher	Oxford University Press
publishDate	2007
url	https://www.ncbi.nlm.nih.gov/pmc/articles/PMC1807962/
_version_	1611394666084696064

Archaeal MCM has separable processivity, substrate choice and helicase domains

Similar Items