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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Elsevier
2007
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| Subjects: |
| _version_ | 1797065965499842560 |
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| author | Moreau, M McGeoch, A Lowe, A Itzhanki, L Bell, S |
| author_facet | Moreau, M McGeoch, A Lowe, A Itzhanki, 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 <em>Sulfolobus solfataricus</em> (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 inter-subunit 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 | 2024-03-06T21:35:46Z |
| format | Journal article |
| id | oxford-uuid:4634ff8f-5355-4133-b5a8-766f1f726389 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T21:35:46Z |
| publishDate | 2007 |
| publisher | Elsevier |
| record_format | dspace |
| spelling | oxford-uuid:4634ff8f-5355-4133-b5a8-766f1f7263892022-03-26T15:12:17ZATPase site architecture and helicase mechanism of an archaeal MCMJournal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:4634ff8f-5355-4133-b5a8-766f1f726389PathologyEnglishOxford University Research Archive - ValetElsevier2007Moreau, MMcGeoch, ALowe, AItzhanki, 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 <em>Sulfolobus solfataricus</em> (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 inter-subunit 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 | Pathology Moreau, M McGeoch, A Lowe, A Itzhanki, 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 |
| topic | Pathology |
| work_keys_str_mv | AT moreaum atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT mcgeocha atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT lowea atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT itzhankil atpasesitearchitectureandhelicasemechanismofanarchaealmcm AT bells atpasesitearchitectureandhelicasemechanismofanarchaealmcm |