gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP
The isolated epsilon subunit of F(1)-ATPase from thermophilic Bacillus PS3 (TF(1)) binds ATP [Y. Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the epsilon subunit even in...
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| Veröffentlicht in: | Biochemical and biophysical research communications 2006-11, Vol.349 (4), p.1368-1371 |
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| container_title | Biochemical and biophysical research communications |
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| creator | Iizuka, Satoshi Kato, Shigeyuki Yoshida, Masasuke Kato-Yamada, Yasuyuki |
| description | The isolated epsilon subunit of F(1)-ATPase from thermophilic Bacillus PS3 (TF(1)) binds ATP [Y. Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the epsilon subunit even in the ATP synthase complex should have the ability to bind ATP. To check if the ATP binding to the epsilon subunit within the ATP synthase complex may occur, the gammaepsilon sub-complex of TF(1) was prepared and ATP binding was examined. The results clearly showed that the gammaepsilon sub-complex can bind ATP. |
| format | Article |
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Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the epsilon subunit even in the ATP synthase complex should have the ability to bind ATP. To check if the ATP binding to the epsilon subunit within the ATP synthase complex may occur, the gammaepsilon sub-complex of TF(1) was prepared and ATP binding was examined. The results clearly showed that the gammaepsilon sub-complex can bind ATP.</description><identifier>ISSN: 0006-291X</identifier><identifier>PMID: 16982032</identifier><language>eng</language><publisher>United States</publisher><subject>Adenosine Triphosphate - chemistry ; Bacillus - enzymology ; Binding Sites ; Enzyme Activation ; Protein Binding ; Protein Structure, Tertiary ; Protein Subunits ; Proton-Translocating ATPases - chemistry</subject><ispartof>Biochemical and biophysical research communications, 2006-11, Vol.349 (4), p.1368-1371</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/16982032$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Iizuka, Satoshi</creatorcontrib><creatorcontrib>Kato, Shigeyuki</creatorcontrib><creatorcontrib>Yoshida, Masasuke</creatorcontrib><creatorcontrib>Kato-Yamada, Yasuyuki</creatorcontrib><title>gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP</title><title>Biochemical and biophysical research communications</title><addtitle>Biochem Biophys Res Commun</addtitle><description>The isolated epsilon subunit of F(1)-ATPase from thermophilic Bacillus PS3 (TF(1)) binds ATP [Y. Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the epsilon subunit even in the ATP synthase complex should have the ability to bind ATP. To check if the ATP binding to the epsilon subunit within the ATP synthase complex may occur, the gammaepsilon sub-complex of TF(1) was prepared and ATP binding was examined. The results clearly showed that the gammaepsilon sub-complex can bind ATP.</description><subject>Adenosine Triphosphate - chemistry</subject><subject>Bacillus - enzymology</subject><subject>Binding Sites</subject><subject>Enzyme Activation</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Protein Subunits</subject><subject>Proton-Translocating ATPases - chemistry</subject><issn>0006-291X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2006</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kDtPwzAYRT2AaCn8BeSJLZLtJH6MVcVLqgSIDGyRHX8hRnYc4kQi_55WLcu9wzm6w71Aa0IIz5iinyt0ndI3IZQWXF2hFeVKMpKzNXr_0iFoGJLzsccfs8maGAYPvzi2eOpgDHHonHcN3lZvOC391OkE-BBHirU5sGnBU8TG9fYo3aDLVvsEt-feoOrxodo9Z_vXp5fddp8NZcEy1VBGCRMCbGFpaZUlAoRteNkypnPBtTQFEUZI3RreAgdeWmaEAQm2zFm-Qfen2WGMPzOkqQ4uNeC97iHOqeZSKiVJcRDvzuJsAth6GF3Q41L_f5D_AaOQV1g</recordid><startdate>20061103</startdate><enddate>20061103</enddate><creator>Iizuka, Satoshi</creator><creator>Kato, Shigeyuki</creator><creator>Yoshida, Masasuke</creator><creator>Kato-Yamada, Yasuyuki</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20061103</creationdate><title>gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP</title><author>Iizuka, Satoshi ; Kato, Shigeyuki ; Yoshida, Masasuke ; Kato-Yamada, Yasuyuki</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p542-9c1210277ed4d15d9d07e7dc65f22a376a8b407b78afb6fe6e65d2b7be8ed5323</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2006</creationdate><topic>Adenosine Triphosphate - chemistry</topic><topic>Bacillus - enzymology</topic><topic>Binding Sites</topic><topic>Enzyme Activation</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Protein Subunits</topic><topic>Proton-Translocating ATPases - chemistry</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Iizuka, Satoshi</creatorcontrib><creatorcontrib>Kato, Shigeyuki</creatorcontrib><creatorcontrib>Yoshida, Masasuke</creatorcontrib><creatorcontrib>Kato-Yamada, Yasuyuki</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Iizuka, Satoshi</au><au>Kato, Shigeyuki</au><au>Yoshida, Masasuke</au><au>Kato-Yamada, Yasuyuki</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>2006-11-03</date><risdate>2006</risdate><volume>349</volume><issue>4</issue><spage>1368</spage><epage>1371</epage><pages>1368-1371</pages><issn>0006-291X</issn><abstract>The isolated epsilon subunit of F(1)-ATPase from thermophilic Bacillus PS3 (TF(1)) binds ATP [Y. Kato-Yamada, M. Yoshida, J. Biol. Chem. 278 (2003) 36013]. The obvious question is whether the ATP binding concern with the regulation of ATP synthase activity or not. If so, the epsilon subunit even in the ATP synthase complex should have the ability to bind ATP. To check if the ATP binding to the epsilon subunit within the ATP synthase complex may occur, the gammaepsilon sub-complex of TF(1) was prepared and ATP binding was examined. The results clearly showed that the gammaepsilon sub-complex can bind ATP.</abstract><cop>United States</cop><pmid>16982032</pmid><tpages>4</tpages></addata></record> |
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| subjects | Adenosine Triphosphate - chemistry Bacillus - enzymology Binding Sites Enzyme Activation Protein Binding Protein Structure, Tertiary Protein Subunits Proton-Translocating ATPases - chemistry |
| title | gammaepsilon Sub-complex of thermophilic ATP synthase has the ability to bind ATP |
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