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Kinesin and Myosin ATPases: Variations on a Theme [and Discussion]
The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less is known about kinesin, but many of its major prop...
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| Published in: | Philosophical transactions of the Royal Society of London. Series B. Biological sciences 1992-04, Vol.336 (1276), p.13-18 |
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| cites | cdi_FETCH-LOGICAL-c556t-7c7758966fd19766d2166eda84beab7b62128e6d61378182f8c015962b72216d3 |
| container_end_page | 18 |
| container_issue | 1276 |
| container_start_page | 13 |
| container_title | Philosophical transactions of the Royal Society of London. Series B. Biological sciences |
| container_volume | 336 |
| creator | Hackney, David D. Johnson, K. A. Hackney, D. D. Holmes, K. C. M.-F. Carlier Elliott, G. F. Burton, K. Trentham, D. R. Cremo, C. |
| description | The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological
structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less
is known about kinesin, but many of its major properties are similar to those of myosin. Both enzymes have two catalytic head
groups at the end of a long $\alpha $-helical rod. The head groups contain the sites for ATP hydrolysis and
interaction with their respective partners for movement (microtubules or F-actin). In each case the binding and hydrolysis
of ATP is rapid and the steady state ATPase rate is limited by a slow step in the region of product release. This slow release
of product is accelerated by interaction with actin or microtubules coupled to changes in binding affinity. As there is no
evidence for a close evolutionary link between kinesin and myosin, these and other similarities may represent convergence
to set of common functional properties which are constrained by the requirements of protein structure and the use of ATP hydrolysis
as a source of energy. It will be of particular interest to determine if these common properties are also shared by the large
number of divergent proteins which have recently been discovered to possess a domain which is homologous to the head group
of kinesin. |
| doi_str_mv | 10.1098/rstb.1992.0038 |
| format | article |
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structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less
is known about kinesin, but many of its major properties are similar to those of myosin. Both enzymes have two catalytic head
groups at the end of a long $\alpha $-helical rod. The head groups contain the sites for ATP hydrolysis and
interaction with their respective partners for movement (microtubules or F-actin). In each case the binding and hydrolysis
of ATP is rapid and the steady state ATPase rate is limited by a slow step in the region of product release. This slow release
of product is accelerated by interaction with actin or microtubules coupled to changes in binding affinity. As there is no
evidence for a close evolutionary link between kinesin and myosin, these and other similarities may represent convergence
to set of common functional properties which are constrained by the requirements of protein structure and the use of ATP hydrolysis
as a source of energy. It will be of particular interest to determine if these common properties are also shared by the large
number of divergent proteins which have recently been discovered to possess a domain which is homologous to the head group
of kinesin.</description><identifier>ISSN: 0962-8436</identifier><identifier>EISSN: 1471-2970</identifier><identifier>DOI: 10.1098/rstb.1992.0038</identifier><identifier>PMID: 1351290</identifier><language>eng</language><publisher>London: The Royal Society</publisher><subject>Actins ; Active sites ; Adenosine triphosphatases ; Adenosine Triphosphate - metabolism ; Dimers ; Enzymes ; Hydrolysis ; Kinesin - chemistry ; Kinesin - metabolism ; Microtubules ; Microtubules - metabolism ; Molecular Structure ; Molecules ; Motors ; Myosins - chemistry ; Myosins - metabolism ; Oxygen ; Protein Conformation</subject><ispartof>Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 1992-04, Vol.336 (1276), p.13-18</ispartof><rights>Copyright 1992 The Royal Society</rights><rights>Scanned images copyright © 2017, Royal Society</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c556t-7c7758966fd19766d2166eda84beab7b62128e6d61378182f8c015962b72216d3</citedby><cites>FETCH-LOGICAL-c556t-7c7758966fd19766d2166eda84beab7b62128e6d61378182f8c015962b72216d3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.jstor.org/stable/pdf/55500$$EPDF$$P50$$Gjstor$$H</linktopdf><linktohtml>$$Uhttps://www.jstor.org/stable/55500$$EHTML$$P50$$Gjstor$$H</linktohtml><link.rule.ids>314,780,784,27922,27923,58236,58469</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1351290$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Hackney, David D.</creatorcontrib><creatorcontrib>Johnson, K. A.</creatorcontrib><creatorcontrib>Hackney, D. D.</creatorcontrib><creatorcontrib>Holmes, K. C.</creatorcontrib><creatorcontrib>M.-F. Carlier</creatorcontrib><creatorcontrib>Elliott, G. F.</creatorcontrib><creatorcontrib>Burton, K.</creatorcontrib><creatorcontrib>Trentham, D. R.</creatorcontrib><creatorcontrib>Cremo, C.</creatorcontrib><title>Kinesin and Myosin ATPases: Variations on a Theme [and Discussion]</title><title>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</title><addtitle>Phil. Trans. R. Soc. Lond. B</addtitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><description>The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological
structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less
is known about kinesin, but many of its major properties are similar to those of myosin. Both enzymes have two catalytic head
groups at the end of a long $\alpha $-helical rod. The head groups contain the sites for ATP hydrolysis and
interaction with their respective partners for movement (microtubules or F-actin). In each case the binding and hydrolysis
of ATP is rapid and the steady state ATPase rate is limited by a slow step in the region of product release. This slow release
of product is accelerated by interaction with actin or microtubules coupled to changes in binding affinity. As there is no
evidence for a close evolutionary link between kinesin and myosin, these and other similarities may represent convergence
to set of common functional properties which are constrained by the requirements of protein structure and the use of ATP hydrolysis
as a source of energy. It will be of particular interest to determine if these common properties are also shared by the large
number of divergent proteins which have recently been discovered to possess a domain which is homologous to the head group
of kinesin.</description><subject>Actins</subject><subject>Active sites</subject><subject>Adenosine triphosphatases</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Dimers</subject><subject>Enzymes</subject><subject>Hydrolysis</subject><subject>Kinesin - chemistry</subject><subject>Kinesin - metabolism</subject><subject>Microtubules</subject><subject>Microtubules - metabolism</subject><subject>Molecular Structure</subject><subject>Molecules</subject><subject>Motors</subject><subject>Myosins - chemistry</subject><subject>Myosins - metabolism</subject><subject>Oxygen</subject><subject>Protein Conformation</subject><issn>0962-8436</issn><issn>1471-2970</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><recordid>eNp9UE1v1DAUtBBVWQpXDkhIOXHL1s9ObIcDUlu-qhaBYOGCkJUPh_UqGwe_BLT8euxNRakQPdlPb2bezBDyCOgSaKGOPY7VEoqCLSnl6g5ZQCYhZYWkd8mCFoKlKuPiHrmPuKGUFrnMDskh8BxYQRfk9ML2Bm2flH2TvN25-D1ZvS_R4LPkc-ltOVrXY-ICIlmtzdYkXyL0hcV6Qgy7rw_IQVt2aB5evUfk06uXq7M36eW71-dnJ5dpnediTGUtZa4KIdoGCilEw0AI05Qqq0xZyUowYMqIRgCXChRrVU0hDwEqyQK04Ufk6aw7ePd9MjjqbTBhuq7sjZtQS05BZYwG4HIG1t4hetPqwdtt6XcaqI6l6ViajqXpWFogPLlSnqqtaa7hc0thj_Peu11I6Gprxp3euMn3YdQfPq5Ogxj9wbmwwKTQVHGgGQMO-pcd9uciQAeAtoiT0XvYTRv_uuK3Xf1vlscza4Oj83-i5HlOY5Djebm239Y_rTf6hnYYhiAWXe79AQ-M57cy4vHa9aPpx795up26Tg9Ny38DhkXMzg</recordid><startdate>19920429</startdate><enddate>19920429</enddate><creator>Hackney, David D.</creator><creator>Johnson, K. A.</creator><creator>Hackney, D. D.</creator><creator>Holmes, K. C.</creator><creator>M.-F. Carlier</creator><creator>Elliott, G. F.</creator><creator>Burton, K.</creator><creator>Trentham, D. R.</creator><creator>Cremo, C.</creator><general>The Royal Society</general><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></search><sort><creationdate>19920429</creationdate><title>Kinesin and Myosin ATPases: Variations on a Theme [and Discussion]</title><author>Hackney, David D. ; Johnson, K. A. ; Hackney, D. D. ; Holmes, K. C. ; M.-F. Carlier ; Elliott, G. F. ; Burton, K. ; Trentham, D. R. ; Cremo, C.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c556t-7c7758966fd19766d2166eda84beab7b62128e6d61378182f8c015962b72216d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Actins</topic><topic>Active sites</topic><topic>Adenosine triphosphatases</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Dimers</topic><topic>Enzymes</topic><topic>Hydrolysis</topic><topic>Kinesin - chemistry</topic><topic>Kinesin - metabolism</topic><topic>Microtubules</topic><topic>Microtubules - metabolism</topic><topic>Molecular Structure</topic><topic>Molecules</topic><topic>Motors</topic><topic>Myosins - chemistry</topic><topic>Myosins - metabolism</topic><topic>Oxygen</topic><topic>Protein Conformation</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Hackney, David D.</creatorcontrib><creatorcontrib>Johnson, K. A.</creatorcontrib><creatorcontrib>Hackney, D. D.</creatorcontrib><creatorcontrib>Holmes, K. C.</creatorcontrib><creatorcontrib>M.-F. Carlier</creatorcontrib><creatorcontrib>Elliott, G. F.</creatorcontrib><creatorcontrib>Burton, K.</creatorcontrib><creatorcontrib>Trentham, D. R.</creatorcontrib><creatorcontrib>Cremo, C.</creatorcontrib><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><jtitle>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Hackney, David D.</au><au>Johnson, K. A.</au><au>Hackney, D. D.</au><au>Holmes, K. C.</au><au>M.-F. Carlier</au><au>Elliott, G. F.</au><au>Burton, K.</au><au>Trentham, D. R.</au><au>Cremo, C.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Kinesin and Myosin ATPases: Variations on a Theme [and Discussion]</atitle><jtitle>Philosophical transactions of the Royal Society of London. Series B. Biological sciences</jtitle><stitle>Phil. Trans. R. Soc. Lond. B</stitle><addtitle>Philos Trans R Soc Lond B Biol Sci</addtitle><date>1992-04-29</date><risdate>1992</risdate><volume>336</volume><issue>1276</issue><spage>13</spage><epage>18</epage><pages>13-18</pages><issn>0962-8436</issn><eissn>1471-2970</eissn><abstract>The enzymes kinesin and myosin are examples of molecular motors which couple ATP hydrolysis to directed movement of biological
structures. Myosin has been extensively studied and its structure and mechanism of coupling are known in detail. Much less
is known about kinesin, but many of its major properties are similar to those of myosin. Both enzymes have two catalytic head
groups at the end of a long $\alpha $-helical rod. The head groups contain the sites for ATP hydrolysis and
interaction with their respective partners for movement (microtubules or F-actin). In each case the binding and hydrolysis
of ATP is rapid and the steady state ATPase rate is limited by a slow step in the region of product release. This slow release
of product is accelerated by interaction with actin or microtubules coupled to changes in binding affinity. As there is no
evidence for a close evolutionary link between kinesin and myosin, these and other similarities may represent convergence
to set of common functional properties which are constrained by the requirements of protein structure and the use of ATP hydrolysis
as a source of energy. It will be of particular interest to determine if these common properties are also shared by the large
number of divergent proteins which have recently been discovered to possess a domain which is homologous to the head group
of kinesin.</abstract><cop>London</cop><pub>The Royal Society</pub><pmid>1351290</pmid><doi>10.1098/rstb.1992.0038</doi><tpages>6</tpages></addata></record> |
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| identifier | ISSN: 0962-8436 |
| ispartof | Philosophical transactions of the Royal Society of London. Series B. Biological sciences, 1992-04, Vol.336 (1276), p.13-18 |
| issn | 0962-8436 1471-2970 |
| language | eng |
| recordid | cdi_jstor_primary_55500 |
| source | JSTOR Archival Journals and Primary Sources Collection; Royal Society Publishing Jisc Collections Royal Society Journals Read & Publish Transitional Agreement 2025 (reading list) |
| subjects | Actins Active sites Adenosine triphosphatases Adenosine Triphosphate - metabolism Dimers Enzymes Hydrolysis Kinesin - chemistry Kinesin - metabolism Microtubules Microtubules - metabolism Molecular Structure Molecules Motors Myosins - chemistry Myosins - metabolism Oxygen Protein Conformation |
| title | Kinesin and Myosin ATPases: Variations on a Theme [and Discussion] |
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