[5] Activation of cholera toxin by ADP-ribosylation factors: 20-kDa guanine nucleotide-binding proteins
This chapter discusses activation of cholera toxin by adenosine diphosphate (ADP)-ribosylation factors. Cholera toxin, a secretory product of Vibrio cholerae, is responsible in large part for the devastating fluid and electrolyte loss characteristic of cholera. The toxin is an oligomeric protein of...
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| Veröffentlicht in: | Methods in Enzymology 1994, Vol.237, p.44-63 |
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| creator | Moss, Joel Haun, Randy S Tsai, Su-Chen Welsh, Catherine F Scott Lee, Fang-Jen Russ Price, S Vaughan, Martha |
| description | This chapter discusses activation of cholera toxin by adenosine diphosphate (ADP)-ribosylation factors. Cholera toxin, a secretory product of Vibrio cholerae, is responsible in large part for the devastating fluid and electrolyte loss characteristic of cholera. The toxin is an oligomeric protein of 84 kDa, consisting of one A subunit (∼29 kDa) and five B subunits (11.6 kDa). The B oligomer is responsible for toxin binding to cell surface ganglioside GM1 [galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosylglucosylceramide]. The A subunit is a latent ADP-ribosyltransferase; activation requires proteolysis near the carboxyl terminus in a domain between two cysteines. Reduction of the disulfide then releases the larger (22 kDa) catalytically active A1 protein (CTA1) and a smaller, carboxyl-terminal A2 protein (CTA2). ADP-ribosylation is responsible for the effects of the toxin on cells. The major ADP-ribose acceptor substrates for the A subunit are the regulatory guanine nucleotide-binding (G) proteins that couple membrane associated cell surface receptors with their intracellular effectors. |
| doi_str_mv | 10.1016/S0076-6879(94)37052-4 |
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Cholera toxin, a secretory product of Vibrio cholerae, is responsible in large part for the devastating fluid and electrolyte loss characteristic of cholera. The toxin is an oligomeric protein of 84 kDa, consisting of one A subunit (∼29 kDa) and five B subunits (11.6 kDa). The B oligomer is responsible for toxin binding to cell surface ganglioside GM1 [galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosylglucosylceramide]. The A subunit is a latent ADP-ribosyltransferase; activation requires proteolysis near the carboxyl terminus in a domain between two cysteines. Reduction of the disulfide then releases the larger (22 kDa) catalytically active A1 protein (CTA1) and a smaller, carboxyl-terminal A2 protein (CTA2). ADP-ribosylation is responsible for the effects of the toxin on cells. The major ADP-ribose acceptor substrates for the A subunit are the regulatory guanine nucleotide-binding (G) proteins that couple membrane associated cell surface receptors with their intracellular effectors.</description><identifier>ISSN: 0076-6879</identifier><identifier>ISBN: 9780121821388</identifier><identifier>ISBN: 0121821382</identifier><identifier>EISSN: 1557-7988</identifier><identifier>DOI: 10.1016/S0076-6879(94)37052-4</identifier><identifier>PMID: 7935017</identifier><language>eng</language><publisher>United States: Elsevier Science & Technology</publisher><subject>Acyltransferases - biosynthesis ; Acyltransferases - metabolism ; Adenosine Diphosphate Ribose - metabolism ; ADP-Ribosylation Factors ; Animals ; Base Sequence ; Brain - metabolism ; Carbon Radioisotopes ; Cattle ; Cell Membrane - metabolism ; Cholera Toxin - metabolism ; Chromatography, Ion Exchange - methods ; Cloning, Molecular - methods ; Cytosol - metabolism ; DNA Primers ; Genes, Fungal ; GTP-Binding Proteins - isolation & purification ; GTP-Binding Proteins - metabolism ; Humans ; Molecular Sequence Data ; Molecular Weight ; NAD - metabolism ; Poly(ADP-ribose) Polymerases - metabolism ; Polymerase Chain Reaction - methods ; Protein Processing, Post-Translational ; Radioisotope Dilution Technique ; Recombinant Proteins - isolation & purification ; Recombinant Proteins - metabolism ; Saccharomyces cerevisiae - enzymology</subject><ispartof>Methods in Enzymology, 1994, Vol.237, p.44-63</ispartof><rights>1994</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0076687994370524$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,775,776,780,789,3445,3536,4009,11268,27902,27903,27904,45789,65309</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/7935017$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Moss, Joel</creatorcontrib><creatorcontrib>Haun, Randy S</creatorcontrib><creatorcontrib>Tsai, Su-Chen</creatorcontrib><creatorcontrib>Welsh, Catherine F</creatorcontrib><creatorcontrib>Scott Lee, Fang-Jen</creatorcontrib><creatorcontrib>Russ Price, S</creatorcontrib><creatorcontrib>Vaughan, Martha</creatorcontrib><title>[5] Activation of cholera toxin by ADP-ribosylation factors: 20-kDa guanine nucleotide-binding proteins</title><title>Methods in Enzymology</title><addtitle>Methods Enzymol</addtitle><description>This chapter discusses activation of cholera toxin by adenosine diphosphate (ADP)-ribosylation factors. Cholera toxin, a secretory product of Vibrio cholerae, is responsible in large part for the devastating fluid and electrolyte loss characteristic of cholera. The toxin is an oligomeric protein of 84 kDa, consisting of one A subunit (∼29 kDa) and five B subunits (11.6 kDa). The B oligomer is responsible for toxin binding to cell surface ganglioside GM1 [galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosylglucosylceramide]. The A subunit is a latent ADP-ribosyltransferase; activation requires proteolysis near the carboxyl terminus in a domain between two cysteines. Reduction of the disulfide then releases the larger (22 kDa) catalytically active A1 protein (CTA1) and a smaller, carboxyl-terminal A2 protein (CTA2). ADP-ribosylation is responsible for the effects of the toxin on cells. The major ADP-ribose acceptor substrates for the A subunit are the regulatory guanine nucleotide-binding (G) proteins that couple membrane associated cell surface receptors with their intracellular effectors.</description><subject>Acyltransferases - biosynthesis</subject><subject>Acyltransferases - metabolism</subject><subject>Adenosine Diphosphate Ribose - metabolism</subject><subject>ADP-Ribosylation Factors</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>Brain - metabolism</subject><subject>Carbon Radioisotopes</subject><subject>Cattle</subject><subject>Cell Membrane - metabolism</subject><subject>Cholera Toxin - metabolism</subject><subject>Chromatography, Ion Exchange - methods</subject><subject>Cloning, Molecular - methods</subject><subject>Cytosol - metabolism</subject><subject>DNA Primers</subject><subject>Genes, Fungal</subject><subject>GTP-Binding Proteins - isolation & purification</subject><subject>GTP-Binding Proteins - metabolism</subject><subject>Humans</subject><subject>Molecular Sequence Data</subject><subject>Molecular Weight</subject><subject>NAD - metabolism</subject><subject>Poly(ADP-ribose) Polymerases - metabolism</subject><subject>Polymerase Chain Reaction - methods</subject><subject>Protein Processing, Post-Translational</subject><subject>Radioisotope Dilution Technique</subject><subject>Recombinant Proteins - isolation & purification</subject><subject>Recombinant Proteins - metabolism</subject><subject>Saccharomyces cerevisiae - enzymology</subject><issn>0076-6879</issn><issn>1557-7988</issn><isbn>9780121821388</isbn><isbn>0121821382</isbn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1994</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kEtLAzEUhYMPaqn9CYUsdRHNc5K4kdL6goKCuhIJySRTo21SZqbF_nv7wrs5i3Pv4Z4PgAHBVwST4voVY1mgQkl9ofklk1hQxI9AlwghkdRKHYO-lgoTShQlTKkT0P0_OQP9pvnGm-GaikJ2QEdqJjCRXTD9EJ9wWLZxZduYE8wVLL_yLNQWtvk3JujWcDh-QXV0uVnP9kuVLdtcNzeQYvQztnC6tCmmANOynIXcRh-Qi8nHNIWLOrchpuYcnFZ21oT-QXvg_f7ubfSIJs8PT6PhBAVa0BZVWFrviArCFwVzXDHOFLG64oIIFziRjmnGqoozuanufOm191IQT2lgyrMeGOxzF0s3D94s6ji39docCm_8270fNk-sYqhNU8aQyuBjHcrW-BwNwWYL3eygmy1Bo7nZQTec_QHb9XC5</recordid><startdate>1994</startdate><enddate>1994</enddate><creator>Moss, Joel</creator><creator>Haun, Randy S</creator><creator>Tsai, Su-Chen</creator><creator>Welsh, Catherine F</creator><creator>Scott Lee, Fang-Jen</creator><creator>Russ Price, S</creator><creator>Vaughan, Martha</creator><general>Elsevier Science & Technology</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope></search><sort><creationdate>1994</creationdate><title>[5] Activation of cholera toxin by ADP-ribosylation factors: 20-kDa guanine nucleotide-binding proteins</title><author>Moss, Joel ; Haun, Randy S ; Tsai, Su-Chen ; Welsh, Catherine F ; Scott Lee, Fang-Jen ; Russ Price, S ; Vaughan, Martha</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-e262t-f07adb18e5d663b4834381a9f4515be417b3933ff437557bdcd9dd751d22e38d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1994</creationdate><topic>Acyltransferases - biosynthesis</topic><topic>Acyltransferases - metabolism</topic><topic>Adenosine Diphosphate Ribose - metabolism</topic><topic>ADP-Ribosylation Factors</topic><topic>Animals</topic><topic>Base Sequence</topic><topic>Brain - metabolism</topic><topic>Carbon Radioisotopes</topic><topic>Cattle</topic><topic>Cell Membrane - metabolism</topic><topic>Cholera Toxin - metabolism</topic><topic>Chromatography, Ion Exchange - methods</topic><topic>Cloning, Molecular - methods</topic><topic>Cytosol - metabolism</topic><topic>DNA Primers</topic><topic>Genes, Fungal</topic><topic>GTP-Binding Proteins - isolation & purification</topic><topic>GTP-Binding Proteins - metabolism</topic><topic>Humans</topic><topic>Molecular Sequence Data</topic><topic>Molecular Weight</topic><topic>NAD - metabolism</topic><topic>Poly(ADP-ribose) Polymerases - metabolism</topic><topic>Polymerase Chain Reaction - methods</topic><topic>Protein Processing, Post-Translational</topic><topic>Radioisotope Dilution Technique</topic><topic>Recombinant Proteins - isolation & purification</topic><topic>Recombinant Proteins - metabolism</topic><topic>Saccharomyces cerevisiae - enzymology</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Moss, Joel</creatorcontrib><creatorcontrib>Haun, Randy S</creatorcontrib><creatorcontrib>Tsai, Su-Chen</creatorcontrib><creatorcontrib>Welsh, Catherine F</creatorcontrib><creatorcontrib>Scott Lee, Fang-Jen</creatorcontrib><creatorcontrib>Russ Price, S</creatorcontrib><creatorcontrib>Vaughan, Martha</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><jtitle>Methods in Enzymology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Moss, Joel</au><au>Haun, Randy S</au><au>Tsai, Su-Chen</au><au>Welsh, Catherine F</au><au>Scott Lee, Fang-Jen</au><au>Russ Price, S</au><au>Vaughan, Martha</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>[5] Activation of cholera toxin by ADP-ribosylation factors: 20-kDa guanine nucleotide-binding proteins</atitle><jtitle>Methods in Enzymology</jtitle><addtitle>Methods Enzymol</addtitle><date>1994</date><risdate>1994</risdate><volume>237</volume><spage>44</spage><epage>63</epage><pages>44-63</pages><issn>0076-6879</issn><eissn>1557-7988</eissn><isbn>9780121821388</isbn><isbn>0121821382</isbn><abstract>This chapter discusses activation of cholera toxin by adenosine diphosphate (ADP)-ribosylation factors. Cholera toxin, a secretory product of Vibrio cholerae, is responsible in large part for the devastating fluid and electrolyte loss characteristic of cholera. The toxin is an oligomeric protein of 84 kDa, consisting of one A subunit (∼29 kDa) and five B subunits (11.6 kDa). The B oligomer is responsible for toxin binding to cell surface ganglioside GM1 [galactosyl-N-acetylgalactosaminyl-(N-acetylneuraminyl) galactosylglucosylceramide]. The A subunit is a latent ADP-ribosyltransferase; activation requires proteolysis near the carboxyl terminus in a domain between two cysteines. Reduction of the disulfide then releases the larger (22 kDa) catalytically active A1 protein (CTA1) and a smaller, carboxyl-terminal A2 protein (CTA2). ADP-ribosylation is responsible for the effects of the toxin on cells. The major ADP-ribose acceptor substrates for the A subunit are the regulatory guanine nucleotide-binding (G) proteins that couple membrane associated cell surface receptors with their intracellular effectors.</abstract><cop>United States</cop><pub>Elsevier Science & Technology</pub><pmid>7935017</pmid><doi>10.1016/S0076-6879(94)37052-4</doi><tpages>20</tpages></addata></record> |
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| subjects | Acyltransferases - biosynthesis Acyltransferases - metabolism Adenosine Diphosphate Ribose - metabolism ADP-Ribosylation Factors Animals Base Sequence Brain - metabolism Carbon Radioisotopes Cattle Cell Membrane - metabolism Cholera Toxin - metabolism Chromatography, Ion Exchange - methods Cloning, Molecular - methods Cytosol - metabolism DNA Primers Genes, Fungal GTP-Binding Proteins - isolation & purification GTP-Binding Proteins - metabolism Humans Molecular Sequence Data Molecular Weight NAD - metabolism Poly(ADP-ribose) Polymerases - metabolism Polymerase Chain Reaction - methods Protein Processing, Post-Translational Radioisotope Dilution Technique Recombinant Proteins - isolation & purification Recombinant Proteins - metabolism Saccharomyces cerevisiae - enzymology |
| title | [5] Activation of cholera toxin by ADP-ribosylation factors: 20-kDa guanine nucleotide-binding proteins |
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