ATPase site architecture and helicase mechanism of an archaeal MCM.
The subunits of the presumptive replicative helicase of archaea and eukaryotes, the MCM complex, are members of the AAA+ (ATPase-associated with various cellular activities) family of ATPases. Proteins within this family harness the chemical energy of ATP hydrolysis to perform a broad range of cellu...
| Main Authors: | , , , , |
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| Format: | Journal article |
| Language: | English |
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2007
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| _version_ | 1826266740192968704 |
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| author | Moreau, M McGeoch, A Lowe, A Itzhaki, L Bell, S |
| author_facet | Moreau, M McGeoch, A Lowe, A Itzhaki, L Bell, S |
| author_sort | Moreau, M |
| collection | OXFORD |
| description | The subunits of the presumptive replicative helicase of archaea and eukaryotes, the MCM complex, are members of the AAA+ (ATPase-associated with various cellular activities) family of ATPases. Proteins within this family harness the chemical energy of ATP hydrolysis to perform a broad range of cellular processes. Here, we investigate the function of the AAA+ site in the mini-chromosome maintenance (MCM) complex of the archaeon Sulfolobus solfataricus (SsoMCM). We find that SsoMCM has an unusual active-site architecture, with a unique blend of features previously found only in distinct families of AAA+ proteins. We additionally describe a series of mutant doping experiments to investigate the mechanistic basis of intersubunit coordination in the generation of helicase activity. Our results indicate that MCM can tolerate catalytically inactive subunits and still function as a helicase, leading us to propose a semisequential model for helicase activity of this complex. |
| first_indexed | 2024-03-06T20:43:33Z |
| format | Journal article |
| id | oxford-uuid:35106f8c-0b7a-4c0a-b1ef-ec8e85ea90d9 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T20:43:33Z |
| publishDate | 2007 |
| record_format | dspace |
| spelling | oxford-uuid:35106f8c-0b7a-4c0a-b1ef-ec8e85ea90d92022-03-26T13:29:55ZATPase site architecture and helicase mechanism of an archaeal MCM.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:35106f8c-0b7a-4c0a-b1ef-ec8e85ea90d9EnglishSymplectic Elements at Oxford2007Moreau, MMcGeoch, ALowe, AItzhaki, LBell, SThe subunits of the presumptive replicative helicase of archaea and eukaryotes, the MCM complex, are members of the AAA+ (ATPase-associated with various cellular activities) family of ATPases. Proteins within this family harness the chemical energy of ATP hydrolysis to perform a broad range of cellular processes. Here, we investigate the function of the AAA+ site in the mini-chromosome maintenance (MCM) complex of the archaeon Sulfolobus solfataricus (SsoMCM). We find that SsoMCM has an unusual active-site architecture, with a unique blend of features previously found only in distinct families of AAA+ proteins. We additionally describe a series of mutant doping experiments to investigate the mechanistic basis of intersubunit coordination in the generation of helicase activity. Our results indicate that MCM can tolerate catalytically inactive subunits and still function as a helicase, leading us to propose a semisequential model for helicase activity of this complex. |
| spellingShingle | Moreau, M McGeoch, A Lowe, A Itzhaki, L Bell, S ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title | ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title_full | ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title_fullStr | ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title_full_unstemmed | ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title_short | ATPase site architecture and helicase mechanism of an archaeal MCM. |
| title_sort | atpase site architecture and helicase mechanism of an archaeal mcm |
| work_keys_str_mv | AT moreaum atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT mcgeocha atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT lowea atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT itzhakil atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT bells atpasesitearchitectureandhelicasemechanismofanarchaealmcm |