A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein
Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities,...
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| Veröffentlicht in: | Journal of structural biology 2014-06, Vol.186 (3), p.367-375 |
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| creator | Gleave, Emma S. Schmidt, Helgo Carter, Andrew P. |
| description | Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor domain generates movement by coupling ATP driven conformational changes in the AAA+ ring to the swing of a motile element called the linker. Dynein binds to its microtubule track via a long antiparallel coiled-coil stalk that emanates from the AAA+ ring. Recently the first high resolution structures of the dynein motor domain were published. Here we provide a detailed structural analysis of the six AAA+ domains using our Saccharomycescerevisiae crystal structure. We describe how structural similarities in the dynein AAA+ domains suggest they share a common evolutionary origin. We analyse how the different AAA+ domains have diverged from each other. We discuss how this is related to the function of dynein as a motor protein and how the AAA+ domains of dynein compare to those of other AAA+ proteins. |
| doi_str_mv | 10.1016/j.jsb.2014.03.019 |
| format | Article |
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The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor domain generates movement by coupling ATP driven conformational changes in the AAA+ ring to the swing of a motile element called the linker. Dynein binds to its microtubule track via a long antiparallel coiled-coil stalk that emanates from the AAA+ ring. Recently the first high resolution structures of the dynein motor domain were published. Here we provide a detailed structural analysis of the six AAA+ domains using our Saccharomycescerevisiae crystal structure. We describe how structural similarities in the dynein AAA+ domains suggest they share a common evolutionary origin. We analyse how the different AAA+ domains have diverged from each other. We discuss how this is related to the function of dynein as a motor protein and how the AAA+ domains of dynein compare to those of other AAA+ proteins.</description><identifier>ISSN: 1047-8477</identifier><identifier>EISSN: 1095-8657</identifier><identifier>DOI: 10.1016/j.jsb.2014.03.019</identifier><identifier>PMID: 24680784</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; ATPases Associated with diverse cellular Activities (AAA+) ; Coiled-coil ; Cytoplasmic Dyneins - chemistry ; Cytoplasmic Dyneins - metabolism ; Cytoskeleton ; Dynein ; Evolution, Molecular ; Microtubule ; Microtubules - metabolism ; Models, Molecular ; Molecular Sequence Data ; Motor protein ; Phylogeny ; Protein Structure, Tertiary ; Saccharomyces cerevisiae ; Saccharomyces cerevisiae Proteins - chemistry ; Saccharomyces cerevisiae Proteins - metabolism ; Sequence Homology, Amino Acid</subject><ispartof>Journal of structural biology, 2014-06, Vol.186 (3), p.367-375</ispartof><rights>2014 The Authors</rights><rights>Copyright © 2014 The Authors. Published by Elsevier Inc. All rights reserved.</rights><rights>2014 The Authors 2014</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c4659-5a493c739a7c89f5a545e196fdbae16bcbf6ce3907c13daa70285532d2585163</citedby><cites>FETCH-LOGICAL-c4659-5a493c739a7c89f5a545e196fdbae16bcbf6ce3907c13daa70285532d2585163</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/j.jsb.2014.03.019$$EHTML$$P50$$Gelsevier$$Hfree_for_read</linktohtml><link.rule.ids>230,314,780,784,885,3550,27924,27925,45995</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24680784$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Gleave, Emma S.</creatorcontrib><creatorcontrib>Schmidt, Helgo</creatorcontrib><creatorcontrib>Carter, Andrew P.</creatorcontrib><title>A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein</title><title>Journal of structural biology</title><addtitle>J Struct Biol</addtitle><description>Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor domain generates movement by coupling ATP driven conformational changes in the AAA+ ring to the swing of a motile element called the linker. Dynein binds to its microtubule track via a long antiparallel coiled-coil stalk that emanates from the AAA+ ring. Recently the first high resolution structures of the dynein motor domain were published. Here we provide a detailed structural analysis of the six AAA+ domains using our Saccharomycescerevisiae crystal structure. We describe how structural similarities in the dynein AAA+ domains suggest they share a common evolutionary origin. We analyse how the different AAA+ domains have diverged from each other. We discuss how this is related to the function of dynein as a motor protein and how the AAA+ domains of dynein compare to those of other AAA+ proteins.</description><subject>Amino Acid Sequence</subject><subject>ATPases Associated with diverse cellular Activities (AAA+)</subject><subject>Coiled-coil</subject><subject>Cytoplasmic Dyneins - chemistry</subject><subject>Cytoplasmic Dyneins - metabolism</subject><subject>Cytoskeleton</subject><subject>Dynein</subject><subject>Evolution, Molecular</subject><subject>Microtubule</subject><subject>Microtubules - metabolism</subject><subject>Models, Molecular</subject><subject>Molecular Sequence Data</subject><subject>Motor protein</subject><subject>Phylogeny</subject><subject>Protein Structure, Tertiary</subject><subject>Saccharomyces cerevisiae</subject><subject>Saccharomyces cerevisiae Proteins - chemistry</subject><subject>Saccharomyces cerevisiae Proteins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><issn>1047-8477</issn><issn>1095-8657</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV2L1TAQhoso7of-AG8kl4K0Js1XgyCURVdhwQv3wruQTqeeHNrmmLQH-u_N4ayL3uhVBvLOOzPvUxSvGK0YZerdvtqnrqopExXlFWXmSXHJqJFlo6R-eqqFLhuh9UVxldKeUipYzZ4XF7VQDdWNuCy-tyQtcYVljW4kbnbjlnwiYSDLDknbtm9JHybn50T8TL45gJ2LYdoAEwGMePTJOySwLeEwujR5IP02o59fFM8GNyZ8-fBeF_efPt7ffC7vvt5-uWnvShBKmlI6YThobpyGxgzSSSGRGTX0nUOmOugGBcgN1cB475ymdSMlr_taNpIpfl18ONse1m7CHnBe8iH2EP3k4maD8_bvn9nv7I9wtCJno2qaDd48GMTwc8W02MknwHF0M4Y1WSYFN6Yxeej_pTyHL4QWWcrOUoghpYjD40aM2hM7u7eZnT2xs5TbzC73vP7zlMeO37Cy4P1ZgDnPo8doE3icAXsfERbbB_8P-19u5arA</recordid><startdate>20140601</startdate><enddate>20140601</enddate><creator>Gleave, Emma S.</creator><creator>Schmidt, Helgo</creator><creator>Carter, Andrew P.</creator><general>Elsevier Inc</general><general>Academic Press</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>M7N</scope><scope>5PM</scope></search><sort><creationdate>20140601</creationdate><title>A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein</title><author>Gleave, Emma S. ; Schmidt, Helgo ; Carter, Andrew P.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c4659-5a493c739a7c89f5a545e196fdbae16bcbf6ce3907c13daa70285532d2585163</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>Amino Acid Sequence</topic><topic>ATPases Associated with diverse cellular Activities (AAA+)</topic><topic>Coiled-coil</topic><topic>Cytoplasmic Dyneins - chemistry</topic><topic>Cytoplasmic Dyneins - metabolism</topic><topic>Cytoskeleton</topic><topic>Dynein</topic><topic>Evolution, Molecular</topic><topic>Microtubule</topic><topic>Microtubules - metabolism</topic><topic>Models, Molecular</topic><topic>Molecular Sequence Data</topic><topic>Motor protein</topic><topic>Phylogeny</topic><topic>Protein Structure, Tertiary</topic><topic>Saccharomyces cerevisiae</topic><topic>Saccharomyces cerevisiae Proteins - chemistry</topic><topic>Saccharomyces cerevisiae Proteins - metabolism</topic><topic>Sequence Homology, Amino Acid</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Gleave, Emma S.</creatorcontrib><creatorcontrib>Schmidt, Helgo</creatorcontrib><creatorcontrib>Carter, Andrew P.</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>Algology Mycology and Protozoology Abstracts (Microbiology C)</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Journal of structural biology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Gleave, Emma S.</au><au>Schmidt, Helgo</au><au>Carter, Andrew P.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein</atitle><jtitle>Journal of structural biology</jtitle><addtitle>J Struct Biol</addtitle><date>2014-06-01</date><risdate>2014</risdate><volume>186</volume><issue>3</issue><spage>367</spage><epage>375</epage><pages>367-375</pages><issn>1047-8477</issn><eissn>1095-8657</eissn><abstract>Dyneins are large protein complexes that act as microtubule based molecular motors. The dynein heavy chain contains a motor domain which is a member of the AAA+ protein family (ATPases Associated with diverse cellular Activities). Proteins of the AAA+ family show a diverse range of functionalities, but share a related core AAA+ domain, which often assembles into hexameric rings. Dynein is unusual because it has all six AAA+ domains linked together, in one long polypeptide. The dynein motor domain generates movement by coupling ATP driven conformational changes in the AAA+ ring to the swing of a motile element called the linker. Dynein binds to its microtubule track via a long antiparallel coiled-coil stalk that emanates from the AAA+ ring. Recently the first high resolution structures of the dynein motor domain were published. Here we provide a detailed structural analysis of the six AAA+ domains using our Saccharomycescerevisiae crystal structure. We describe how structural similarities in the dynein AAA+ domains suggest they share a common evolutionary origin. 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| language | eng |
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| subjects | Amino Acid Sequence ATPases Associated with diverse cellular Activities (AAA+) Coiled-coil Cytoplasmic Dyneins - chemistry Cytoplasmic Dyneins - metabolism Cytoskeleton Dynein Evolution, Molecular Microtubule Microtubules - metabolism Models, Molecular Molecular Sequence Data Motor protein Phylogeny Protein Structure, Tertiary Saccharomyces cerevisiae Saccharomyces cerevisiae Proteins - chemistry Saccharomyces cerevisiae Proteins - metabolism Sequence Homology, Amino Acid |
| title | A structural analysis of the AAA+ domains in Saccharomyces cerevisiae cytoplasmic dynein |
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