Interaction between cGMP-phosphodiesterase and transducin alpha-subunit in retinal rods. A cross-linking study
Cross-linking of the different subunits of the retinal cGMP-phosphodiesterase (PDE) with its activator G alpha GTP gamma S (alpha subunit of the retinal G-protein transducin with GTP gamma S (guanosine 5'-O-(3-thiotriphosphate) bound) has been investigated using purified proteins, with a N-hydr...
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| Veröffentlicht in: | The Journal of biological chemistry 1992-10, Vol.267 (28), p.19948-19953 |
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| container_title | The Journal of biological chemistry |
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| creator | CLERC, A CATTY, P BENNETT, N |
| description | Cross-linking of the different subunits of the retinal cGMP-phosphodiesterase (PDE) with its activator G alpha GTP gamma S
(alpha subunit of the retinal G-protein transducin with GTP gamma S (guanosine 5'-O-(3-thiotriphosphate) bound) has been investigated
using purified proteins, with a N-hydroxysuccinimide homobifunctional cross-linker, bis(sulfosuccinimidyl)suberate (BS3) and
its cleavable analog 3,3'-dithiobis(sulfosuccinimidylpropionate) (DTSSP). Interaction of purified G-protein and PDE is achieved
in the presence of lecithin vesicles, at protein concentrations sufficient for full PDE activation. Protein subunits linked
with DTSSP are separated by cleavage of the disulfide bridge and identified by electrophoresis. Complexes of PDE alpha (PDE
beta) with 1 and 2 molecules of activator G alpha GTP gamma S are observed, providing direct evidence for an interaction or
at least a close proximity between 2 molecules of activator G alpha and each of the catalytic PDE subunits in the activated
state of PDE. The results also reveal symmetrical roles of PDE alpha and PDE beta, with the existence of one site for PDE
gamma and one site for G alpha on each catalytic subunit. |
| doi_str_mv | 10.1016/S0021-9258(19)88649-0 |
| format | Article |
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(alpha subunit of the retinal G-protein transducin with GTP gamma S (guanosine 5'-O-(3-thiotriphosphate) bound) has been investigated
using purified proteins, with a N-hydroxysuccinimide homobifunctional cross-linker, bis(sulfosuccinimidyl)suberate (BS3) and
its cleavable analog 3,3'-dithiobis(sulfosuccinimidylpropionate) (DTSSP). Interaction of purified G-protein and PDE is achieved
in the presence of lecithin vesicles, at protein concentrations sufficient for full PDE activation. Protein subunits linked
with DTSSP are separated by cleavage of the disulfide bridge and identified by electrophoresis. Complexes of PDE alpha (PDE
beta) with 1 and 2 molecules of activator G alpha GTP gamma S are observed, providing direct evidence for an interaction or
at least a close proximity between 2 molecules of activator G alpha and each of the catalytic PDE subunits in the activated
state of PDE. The results also reveal symmetrical roles of PDE alpha and PDE beta, with the existence of one site for PDE
gamma and one site for G alpha on each catalytic subunit.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1016/S0021-9258(19)88649-0</identifier><identifier>PMID: 1328188</identifier><identifier>CODEN: JBCHA3</identifier><language>eng</language><publisher>Bethesda, MD: American Society for Biochemistry and Molecular Biology</publisher><subject>3',5'-cyclic-GMP phosphodiesterase ; 3',5'-Cyclic-GMP Phosphodiesterases - metabolism ; alpha subunits ; Animals ; Biological and medical sciences ; Cattle ; Cell physiology ; Cross-Linking Reagents ; Disulfides - chemistry ; Electrophoresis, Polyacrylamide Gel ; Enzyme Activation ; Fundamental and applied biological sciences. Psychology ; GTP-Binding Proteins - metabolism ; Guanosine 5'-O-(3-Thiotriphosphate) - metabolism ; interaction ; Molecular and cellular biology ; photoreceptors ; Rod Cell Outer Segment - enzymology ; Rod Cell Outer Segment - metabolism ; rods ; Succinimides ; transducin ; Transducin - metabolism ; Vision, photoreception</subject><ispartof>The Journal of biological chemistry, 1992-10, Vol.267 (28), p.19948-19953</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c440t-7b346bf0a9f319ff1ec00b97e24ee6d2f045886d69db15a3cd9a42ed9ca90efe3</citedby><cites>FETCH-LOGICAL-c440t-7b346bf0a9f319ff1ec00b97e24ee6d2f045886d69db15a3cd9a42ed9ca90efe3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4402385$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1328188$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>CLERC, A</creatorcontrib><creatorcontrib>CATTY, P</creatorcontrib><creatorcontrib>BENNETT, N</creatorcontrib><title>Interaction between cGMP-phosphodiesterase and transducin alpha-subunit in retinal rods. A cross-linking study</title><title>The Journal of biological chemistry</title><addtitle>J Biol Chem</addtitle><description>Cross-linking of the different subunits of the retinal cGMP-phosphodiesterase (PDE) with its activator G alpha GTP gamma S
(alpha subunit of the retinal G-protein transducin with GTP gamma S (guanosine 5'-O-(3-thiotriphosphate) bound) has been investigated
using purified proteins, with a N-hydroxysuccinimide homobifunctional cross-linker, bis(sulfosuccinimidyl)suberate (BS3) and
its cleavable analog 3,3'-dithiobis(sulfosuccinimidylpropionate) (DTSSP). Interaction of purified G-protein and PDE is achieved
in the presence of lecithin vesicles, at protein concentrations sufficient for full PDE activation. Protein subunits linked
with DTSSP are separated by cleavage of the disulfide bridge and identified by electrophoresis. Complexes of PDE alpha (PDE
beta) with 1 and 2 molecules of activator G alpha GTP gamma S are observed, providing direct evidence for an interaction or
at least a close proximity between 2 molecules of activator G alpha and each of the catalytic PDE subunits in the activated
state of PDE. The results also reveal symmetrical roles of PDE alpha and PDE beta, with the existence of one site for PDE
gamma and one site for G alpha on each catalytic subunit.</description><subject>3',5'-cyclic-GMP phosphodiesterase</subject><subject>3',5'-Cyclic-GMP Phosphodiesterases - metabolism</subject><subject>alpha subunits</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Cell physiology</subject><subject>Cross-Linking Reagents</subject><subject>Disulfides - chemistry</subject><subject>Electrophoresis, Polyacrylamide Gel</subject><subject>Enzyme Activation</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Guanosine 5'-O-(3-Thiotriphosphate) - metabolism</subject><subject>interaction</subject><subject>Molecular and cellular biology</subject><subject>photoreceptors</subject><subject>Rod Cell Outer Segment - enzymology</subject><subject>Rod Cell Outer Segment - metabolism</subject><subject>rods</subject><subject>Succinimides</subject><subject>transducin</subject><subject>Transducin - metabolism</subject><subject>Vision, photoreception</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkV1rFDEYhYModa3-hEIuRPQiNV8zk1yWUmuhoqCCdyGTvOlEZzNrMkPpvzezu7SXBkIg75MczjkInTF6zihrP36nlDOieaPeM_1BqVZqQp-hDaNKENGwX8_R5hF5iV6V8pvWJTU7QSdMcMWU2qB0k2bI1s1xSriH-R4gYXf95RvZDVOp20coK1EA2-TxnG0qfnExYTvuBkvK0i8pzrheZJhjsiPOky_n-AK7PJVCxpj-xHSHy7z4h9foRbBjgTfH8xT9_HT14_Izuf16fXN5cUuclHQmXS9k2wdqdRBMh8DAUdrrDrgEaD0PVDbVsW-171ljhfPaSg5eO6spBBCn6N3h312e_i7VgdnG4mAcbYJpKaYTnAvW0v-CrJWsE01XweYA7l1lCGaX49bmB8OoWQsx-0LMmrZh2uwLMavA2VFg6bfgn14dGqjzt8e5Lc6OoebrYnnEahxcqOYJG-LdcB8zmD5OboCt4W1n-CqppRL_AI2loTE</recordid><startdate>19921005</startdate><enddate>19921005</enddate><creator>CLERC, A</creator><creator>CATTY, P</creator><creator>BENNETT, N</creator><general>American Society for Biochemistry and Molecular Biology</general><scope>IQODW</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>8FD</scope><scope>FR3</scope><scope>M7Z</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19921005</creationdate><title>Interaction between cGMP-phosphodiesterase and transducin alpha-subunit in retinal rods. A cross-linking study</title><author>CLERC, A ; CATTY, P ; BENNETT, N</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c440t-7b346bf0a9f319ff1ec00b97e24ee6d2f045886d69db15a3cd9a42ed9ca90efe3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>3',5'-cyclic-GMP phosphodiesterase</topic><topic>3',5'-Cyclic-GMP Phosphodiesterases - metabolism</topic><topic>alpha subunits</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cattle</topic><topic>Cell physiology</topic><topic>Cross-Linking Reagents</topic><topic>Disulfides - chemistry</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>Enzyme Activation</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Guanosine 5'-O-(3-Thiotriphosphate) - metabolism</topic><topic>interaction</topic><topic>Molecular and cellular biology</topic><topic>photoreceptors</topic><topic>Rod Cell Outer Segment - enzymology</topic><topic>Rod Cell Outer Segment - metabolism</topic><topic>rods</topic><topic>Succinimides</topic><topic>transducin</topic><topic>Transducin - metabolism</topic><topic>Vision, photoreception</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>CLERC, A</creatorcontrib><creatorcontrib>CATTY, P</creatorcontrib><creatorcontrib>BENNETT, N</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biochemistry Abstracts 1</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>CLERC, A</au><au>CATTY, P</au><au>BENNETT, N</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Interaction between cGMP-phosphodiesterase and transducin alpha-subunit in retinal rods. A cross-linking study</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>1992-10-05</date><risdate>1992</risdate><volume>267</volume><issue>28</issue><spage>19948</spage><epage>19953</epage><pages>19948-19953</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><coden>JBCHA3</coden><abstract>Cross-linking of the different subunits of the retinal cGMP-phosphodiesterase (PDE) with its activator G alpha GTP gamma S
(alpha subunit of the retinal G-protein transducin with GTP gamma S (guanosine 5'-O-(3-thiotriphosphate) bound) has been investigated
using purified proteins, with a N-hydroxysuccinimide homobifunctional cross-linker, bis(sulfosuccinimidyl)suberate (BS3) and
its cleavable analog 3,3'-dithiobis(sulfosuccinimidylpropionate) (DTSSP). Interaction of purified G-protein and PDE is achieved
in the presence of lecithin vesicles, at protein concentrations sufficient for full PDE activation. Protein subunits linked
with DTSSP are separated by cleavage of the disulfide bridge and identified by electrophoresis. Complexes of PDE alpha (PDE
beta) with 1 and 2 molecules of activator G alpha GTP gamma S are observed, providing direct evidence for an interaction or
at least a close proximity between 2 molecules of activator G alpha and each of the catalytic PDE subunits in the activated
state of PDE. The results also reveal symmetrical roles of PDE alpha and PDE beta, with the existence of one site for PDE
gamma and one site for G alpha on each catalytic subunit.</abstract><cop>Bethesda, MD</cop><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>1328188</pmid><doi>10.1016/S0021-9258(19)88649-0</doi><tpages>6</tpages><oa>free_for_read</oa></addata></record> |
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| language | eng |
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| source | MEDLINE; EZB-FREE-00999 freely available EZB journals; Alma/SFX Local Collection |
| subjects | 3',5'-cyclic-GMP phosphodiesterase 3',5'-Cyclic-GMP Phosphodiesterases - metabolism alpha subunits Animals Biological and medical sciences Cattle Cell physiology Cross-Linking Reagents Disulfides - chemistry Electrophoresis, Polyacrylamide Gel Enzyme Activation Fundamental and applied biological sciences. Psychology GTP-Binding Proteins - metabolism Guanosine 5'-O-(3-Thiotriphosphate) - metabolism interaction Molecular and cellular biology photoreceptors Rod Cell Outer Segment - enzymology Rod Cell Outer Segment - metabolism rods Succinimides transducin Transducin - metabolism Vision, photoreception |
| title | Interaction between cGMP-phosphodiesterase and transducin alpha-subunit in retinal rods. A cross-linking study |
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