Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation
F 1 -ATPase (F 1 ) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F 1 that was characterized by a rate constant remarkably sensiti...
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| Veröffentlicht in: | Scientific reports 2014-05, Vol.4 (1), p.4962-4962, Article 4962 |
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| creator | Watanabe, Rikiya Noji, Hiroyuki |
| description | F
1
-ATPase (F
1
) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F
1
that was characterized by a rate constant remarkably sensitive to temperature and had a Q
10
factor of 6–19. Since reactions with high Q
10
values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F
1
. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F
1
. |
| doi_str_mv | 10.1038/srep04962 |
| format | Article |
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1
-ATPase (F
1
) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F
1
that was characterized by a rate constant remarkably sensitive to temperature and had a Q
10
factor of 6–19. Since reactions with high Q
10
values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F
1
. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F
1
.</description><identifier>ISSN: 2045-2322</identifier><identifier>EISSN: 2045-2322</identifier><identifier>DOI: 10.1038/srep04962</identifier><identifier>PMID: 24825532</identifier><language>eng</language><publisher>London: Nature Publishing Group UK</publisher><subject>631/57/1464 ; 631/57/2265 ; Adenosine triphosphatase ; Adenosine Triphosphate - chemistry ; Adenosine Triphosphate - metabolism ; Catalysis ; Equilibrium ; F1-ATPase ; Humanities and Social Sciences ; Hydrolysis ; Kinetics ; Molecular Motor Proteins - chemistry ; Molecular Motor Proteins - metabolism ; Motor task performance ; multidisciplinary ; Proton-Translocating ATPases - chemistry ; Proton-Translocating ATPases - metabolism ; Rotation ; Science ; Temperature ; Temperature effects ; Torque</subject><ispartof>Scientific reports, 2014-05, Vol.4 (1), p.4962-4962, Article 4962</ispartof><rights>The Author(s) 2014</rights><rights>Copyright Nature Publishing Group May 2014</rights><rights>Copyright © 2014, Macmillan Publishers Limited. All rights reserved 2014 Macmillan Publishers Limited. All rights reserved</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c504t-2165b7d90b83fc45f3687e95b1b9169a8955cbed081294e131c57e819f5099b53</citedby><cites>FETCH-LOGICAL-c504t-2165b7d90b83fc45f3687e95b1b9169a8955cbed081294e131c57e819f5099b53</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019956/pdf/$$EPDF$$P50$$Gpubmedcentral$$Hfree_for_read</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC4019956/$$EHTML$$P50$$Gpubmedcentral$$Hfree_for_read</linktohtml><link.rule.ids>230,314,723,776,780,860,881,27901,27902,41096,42165,51551,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/24825532$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Watanabe, Rikiya</creatorcontrib><creatorcontrib>Noji, Hiroyuki</creatorcontrib><title>Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation</title><title>Scientific reports</title><addtitle>Sci Rep</addtitle><addtitle>Sci Rep</addtitle><description>F
1
-ATPase (F
1
) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F
1
that was characterized by a rate constant remarkably sensitive to temperature and had a Q
10
factor of 6–19. Since reactions with high Q
10
values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F
1
. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F
1
.</description><subject>631/57/1464</subject><subject>631/57/2265</subject><subject>Adenosine triphosphatase</subject><subject>Adenosine Triphosphate - chemistry</subject><subject>Adenosine Triphosphate - metabolism</subject><subject>Catalysis</subject><subject>Equilibrium</subject><subject>F1-ATPase</subject><subject>Humanities and Social Sciences</subject><subject>Hydrolysis</subject><subject>Kinetics</subject><subject>Molecular Motor Proteins - chemistry</subject><subject>Molecular Motor Proteins - metabolism</subject><subject>Motor task performance</subject><subject>multidisciplinary</subject><subject>Proton-Translocating ATPases - chemistry</subject><subject>Proton-Translocating ATPases - metabolism</subject><subject>Rotation</subject><subject>Science</subject><subject>Temperature</subject><subject>Temperature effects</subject><subject>Torque</subject><issn>2045-2322</issn><issn>2045-2322</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2014</creationdate><recordtype>article</recordtype><sourceid>C6C</sourceid><sourceid>EIF</sourceid><sourceid>BENPR</sourceid><recordid>eNplkUFLHDEUx0NRqlgP_QIy4EWFqXmZyWxyKchSbUHQgz2HTPbNbmQmGZOMoJ_e2N0ua5tDEng_fnkvf0K-Av0GtBKXMeBIa9mwT-SQ0ZqXrGJsb-d-QI5jfKR5cSZrkJ_JAasF47xih8TOVzpokzDYV52sd4XvirTCIuEwYtBpClhGdNEm-4xFwMxuqGsorx7udcSifSmmaN2yeN96LAffo5l6LAbt7Dj1f8RfyH6n-4jHm_OI_L7-8TD_Wd7e3fyaX92WhtM6lQwa3s4Wkrai6kzNu6oRM5S8hVZCI7WQnJsWF1RAngahAsNnKEB2nErZ8uqIfF97x6kdcGHQpaB7NQY76PCivLbqY8XZlVr6Z1VTkJI3WXC2EQT_NGFMarDRYN9rh36KCnj-PpjxCjJ6-g_66Kfg8ngKhBSUShAiU-drygQfc1zdthmg6j1Dtc0wsye73W_Jv4ll4GINxFxySww7T_5newNM0aaX</recordid><startdate>20140514</startdate><enddate>20140514</enddate><creator>Watanabe, Rikiya</creator><creator>Noji, Hiroyuki</creator><general>Nature Publishing Group UK</general><general>Nature Publishing Group</general><scope>C6C</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>3V.</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>PIMPY</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>PRINS</scope><scope>Q9U</scope><scope>7X8</scope><scope>5PM</scope></search><sort><creationdate>20140514</creationdate><title>Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation</title><author>Watanabe, Rikiya ; Noji, Hiroyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c504t-2165b7d90b83fc45f3687e95b1b9169a8955cbed081294e131c57e819f5099b53</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2014</creationdate><topic>631/57/1464</topic><topic>631/57/2265</topic><topic>Adenosine triphosphatase</topic><topic>Adenosine Triphosphate - chemistry</topic><topic>Adenosine Triphosphate - metabolism</topic><topic>Catalysis</topic><topic>Equilibrium</topic><topic>F1-ATPase</topic><topic>Humanities and Social Sciences</topic><topic>Hydrolysis</topic><topic>Kinetics</topic><topic>Molecular Motor Proteins - chemistry</topic><topic>Molecular Motor Proteins - metabolism</topic><topic>Motor task performance</topic><topic>multidisciplinary</topic><topic>Proton-Translocating ATPases - chemistry</topic><topic>Proton-Translocating ATPases - metabolism</topic><topic>Rotation</topic><topic>Science</topic><topic>Temperature</topic><topic>Temperature effects</topic><topic>Torque</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Watanabe, Rikiya</creatorcontrib><creatorcontrib>Noji, Hiroyuki</creatorcontrib><collection>Springer Nature OA Free Journals</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Publicly Available Content Database</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central China</collection><collection>ProQuest Central Basic</collection><collection>MEDLINE - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>Scientific reports</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Watanabe, Rikiya</au><au>Noji, Hiroyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation</atitle><jtitle>Scientific reports</jtitle><stitle>Sci Rep</stitle><addtitle>Sci Rep</addtitle><date>2014-05-14</date><risdate>2014</risdate><volume>4</volume><issue>1</issue><spage>4962</spage><epage>4962</epage><pages>4962-4962</pages><artnum>4962</artnum><issn>2045-2322</issn><eissn>2045-2322</eissn><abstract>F
1
-ATPase (F
1
) is a rotary motor protein that couples ATP hydrolysis to mechanical rotation with high efficiency. In our recent study, we observed a highly temperature-sensitive (TS) step in the reaction catalyzed by a thermophilic F
1
that was characterized by a rate constant remarkably sensitive to temperature and had a Q
10
factor of 6–19. Since reactions with high Q
10
values are considered to involve large conformational changes, we speculated that the TS reaction plays a key role in the rotation of F
1
. To clarify the role of the TS reaction, in this study, we conducted a stall and release experiment using magnetic tweezers and assessed the torque generated during the TS reaction. The results indicate that the TS reaction generates the same amount of rotational torque as does ATP binding, but more than that generated during ATP hydrolysis. Thus, we confirmed that the TS reaction contributes significantly to the rotation of F
1
.</abstract><cop>London</cop><pub>Nature Publishing Group UK</pub><pmid>24825532</pmid><doi>10.1038/srep04962</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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| subjects | 631/57/1464 631/57/2265 Adenosine triphosphatase Adenosine Triphosphate - chemistry Adenosine Triphosphate - metabolism Catalysis Equilibrium F1-ATPase Humanities and Social Sciences Hydrolysis Kinetics Molecular Motor Proteins - chemistry Molecular Motor Proteins - metabolism Motor task performance multidisciplinary Proton-Translocating ATPases - chemistry Proton-Translocating ATPases - metabolism Rotation Science Temperature Temperature effects Torque |
| title | Characterization of the temperature-sensitive reaction of F1-ATPase by using single-molecule manipulation |
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