Application of an N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine-substituted peptide as a heterobifunctional cross-linking agent in a study of protein O-glycosylation in yeast
In order to investigate the O-mannosyltransferase involved in the initial O-mannosylation of glycoproteins in Saccharomyces cerevisiae, a photoactive hexapeptide, [125I]-N-(4-azido-2,3,5,6-tetrafluorobenzoyl)-3-iodo-Tyr-Asn-Pro-T hr-Ser-Val ([125I]azidoTyr-peptide), was synthesized by solid-phase te...
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| Veröffentlicht in: | Bioconjugate chemistry 1992-01, Vol.3 (1), p.69-73 |
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| container_title | Bioconjugate chemistry |
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| creator | Drake, Richard R. Slama, James T. Wall, Katherine A. Abramova, Margaret D'Souza, Crislyn Elbein, Alan D. Crocker, Peter J. Watt, David S. |
| description | In order to investigate the O-mannosyltransferase involved in the initial O-mannosylation of glycoproteins in Saccharomyces cerevisiae, a photoactive hexapeptide, [125I]-N-(4-azido-2,3,5,6-tetrafluorobenzoyl)-3-iodo-Tyr-Asn-Pro-T hr-Ser-Val ([125I]azidoTyr-peptide), was synthesized by solid-phase techniques using a new photoactive cross-linking reagent, N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine, and resin-bound Asn-Pro-Thr(tBu)-Ser(tBu)-Val. When this modified hexapeptide substrate was incubated with O-mannosyltransferase preparations, the hexapeptide was an acceptor of [14C]-mannose from dolichol phosphate-[14C]mannose. After partially purifying the O-mannosyltransferase and photolabeling these enzyme preparations with [125I]azidoTyr-peptide, a ca. 82-kDa protein was shown to be the only apparent photolabeled protein that was protected by unmodified hexapeptide. This ca. 82-kDa protein may be the catalytic subunit of the O-mannosyltransferase. The susceptibility of the N-(4-azido-2,3,5,6-tetrafluorobenzoyl) moiety to reducing agents in aqueous buffers was also examined. |
| doi_str_mv | 10.1021/bc00013a011 |
| format | Article |
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When this modified hexapeptide substrate was incubated with O-mannosyltransferase preparations, the hexapeptide was an acceptor of [14C]-mannose from dolichol phosphate-[14C]mannose. After partially purifying the O-mannosyltransferase and photolabeling these enzyme preparations with [125I]azidoTyr-peptide, a ca. 82-kDa protein was shown to be the only apparent photolabeled protein that was protected by unmodified hexapeptide. This ca. 82-kDa protein may be the catalytic subunit of the O-mannosyltransferase. The susceptibility of the N-(4-azido-2,3,5,6-tetrafluorobenzoyl) moiety to reducing agents in aqueous buffers was also examined.</description><identifier>ISSN: 1043-1802</identifier><identifier>EISSN: 1520-4812</identifier><identifier>DOI: 10.1021/bc00013a011</identifier><identifier>PMID: 1616952</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Amino Acid Sequence ; Analytical, structural and metabolic biochemistry ; Azides - chemistry ; Azides - metabolism ; Biological and medical sciences ; Cross-Linking Reagents ; Enzymes and enzyme inhibitors ; Fundamental and applied biological sciences. Psychology ; Fungal Proteins - metabolism ; Glycoproteins - metabolism ; Glycosylation ; Mannosyltransferases - metabolism ; Molecular Sequence Data ; Saccharomyces cerevisiae - metabolism ; Spectrophotometry, Ultraviolet ; Tyrosine - analogs & derivatives ; Tyrosine - chemistry ; Tyrosine - metabolism</subject><ispartof>Bioconjugate chemistry, 1992-01, Vol.3 (1), p.69-73</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a383t-f21eda326c2dc03a024ab3bd9a554917fea897215f474637224caadaa5b35b223</citedby></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://pubs.acs.org/doi/pdf/10.1021/bc00013a011$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bc00013a011$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,776,780,2752,4010,27053,27900,27901,27902,56713,56763</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4347985$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/1616952$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Drake, Richard R.</creatorcontrib><creatorcontrib>Slama, James T.</creatorcontrib><creatorcontrib>Wall, Katherine A.</creatorcontrib><creatorcontrib>Abramova, Margaret</creatorcontrib><creatorcontrib>D'Souza, Crislyn</creatorcontrib><creatorcontrib>Elbein, Alan D.</creatorcontrib><creatorcontrib>Crocker, Peter J.</creatorcontrib><creatorcontrib>Watt, David S.</creatorcontrib><title>Application of an N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine-substituted peptide as a heterobifunctional cross-linking agent in a study of protein O-glycosylation in yeast</title><title>Bioconjugate chemistry</title><addtitle>Bioconjugate Chem</addtitle><description>In order to investigate the O-mannosyltransferase involved in the initial O-mannosylation of glycoproteins in Saccharomyces cerevisiae, a photoactive hexapeptide, [125I]-N-(4-azido-2,3,5,6-tetrafluorobenzoyl)-3-iodo-Tyr-Asn-Pro-T hr-Ser-Val ([125I]azidoTyr-peptide), was synthesized by solid-phase techniques using a new photoactive cross-linking reagent, N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine, and resin-bound Asn-Pro-Thr(tBu)-Ser(tBu)-Val. When this modified hexapeptide substrate was incubated with O-mannosyltransferase preparations, the hexapeptide was an acceptor of [14C]-mannose from dolichol phosphate-[14C]mannose. After partially purifying the O-mannosyltransferase and photolabeling these enzyme preparations with [125I]azidoTyr-peptide, a ca. 82-kDa protein was shown to be the only apparent photolabeled protein that was protected by unmodified hexapeptide. This ca. 82-kDa protein may be the catalytic subunit of the O-mannosyltransferase. The susceptibility of the N-(4-azido-2,3,5,6-tetrafluorobenzoyl) moiety to reducing agents in aqueous buffers was also examined.</description><subject>Amino Acid Sequence</subject><subject>Analytical, structural and metabolic biochemistry</subject><subject>Azides - chemistry</subject><subject>Azides - metabolism</subject><subject>Biological and medical sciences</subject><subject>Cross-Linking Reagents</subject><subject>Enzymes and enzyme inhibitors</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Fungal Proteins - metabolism</subject><subject>Glycoproteins - metabolism</subject><subject>Glycosylation</subject><subject>Mannosyltransferases - metabolism</subject><subject>Molecular Sequence Data</subject><subject>Saccharomyces cerevisiae - metabolism</subject><subject>Spectrophotometry, Ultraviolet</subject><subject>Tyrosine - analogs & derivatives</subject><subject>Tyrosine - chemistry</subject><subject>Tyrosine - metabolism</subject><issn>1043-1802</issn><issn>1520-4812</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1992</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNptkUtv1TAQhSMEKm1hxRrJC0RBXIMfcR7LqqK0UFEkCltr4jgXt752sB2J9E_xF_FtrgoLVrbmfJ45nlMUzyh5Swmj7zpFCKEcCKUPin0qGMFlQ9nDfCclx7Qh7HFxEON1xlrasL1ij1a0agXbL34fj6M1CpLxDvkBgUOf8asSw63pPWYrvhKrCiedAgx28sF32t362b5Oc_DROI3j1MVk0pR0j0Y9JtNrBBEB-qGTzrwZJqe27cEild9EbI27MW6NYK1dQsZlNqapn7fzx-CTzqVLvLaz8nG2i7VcmjXE9KR4NICN-unuPCy-nb6_OjnDF5cfzk-OLzDwhic8MKp74KxSrFckr4aV0PGub0GIsqX1oKFpa0bFUNZlxWvGSgXQA4iOi44xfli8XPpmQz8nHZPcmKi0teC0n6KseV5tyUgG3yzg3d-CHuQYzAbCLCmR23jkP_Fk-vmu7dRtdP-XXfLI-oudDlGBHQI4ZeI9lkfWbSMyhhfMxKR_3csQbmRV81rIqy9fJT_7_ol-PKWyyvzRwoOK8tpPIYcR_2vwD9AOtTY</recordid><startdate>19920101</startdate><enddate>19920101</enddate><creator>Drake, Richard R.</creator><creator>Slama, James T.</creator><creator>Wall, Katherine A.</creator><creator>Abramova, Margaret</creator><creator>D'Souza, Crislyn</creator><creator>Elbein, Alan D.</creator><creator>Crocker, Peter J.</creator><creator>Watt, David S.</creator><general>American Chemical Society</general><scope>BSCLL</scope><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>7X8</scope></search><sort><creationdate>19920101</creationdate><title>Application of an N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine-substituted peptide as a heterobifunctional cross-linking agent in a study of protein O-glycosylation in yeast</title><author>Drake, Richard R. ; Slama, James T. ; Wall, Katherine A. ; Abramova, Margaret ; D'Souza, Crislyn ; Elbein, Alan D. ; Crocker, Peter J. ; Watt, David S.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-a383t-f21eda326c2dc03a024ab3bd9a554917fea897215f474637224caadaa5b35b223</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1992</creationdate><topic>Amino Acid Sequence</topic><topic>Analytical, structural and metabolic biochemistry</topic><topic>Azides - chemistry</topic><topic>Azides - metabolism</topic><topic>Biological and medical sciences</topic><topic>Cross-Linking Reagents</topic><topic>Enzymes and enzyme inhibitors</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Fungal Proteins - metabolism</topic><topic>Glycoproteins - metabolism</topic><topic>Glycosylation</topic><topic>Mannosyltransferases - metabolism</topic><topic>Molecular Sequence Data</topic><topic>Saccharomyces cerevisiae - metabolism</topic><topic>Spectrophotometry, Ultraviolet</topic><topic>Tyrosine - analogs & derivatives</topic><topic>Tyrosine - chemistry</topic><topic>Tyrosine - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Drake, Richard R.</creatorcontrib><creatorcontrib>Slama, James T.</creatorcontrib><creatorcontrib>Wall, Katherine A.</creatorcontrib><creatorcontrib>Abramova, Margaret</creatorcontrib><creatorcontrib>D'Souza, Crislyn</creatorcontrib><creatorcontrib>Elbein, Alan D.</creatorcontrib><creatorcontrib>Crocker, Peter J.</creatorcontrib><creatorcontrib>Watt, David S.</creatorcontrib><collection>Istex</collection><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>MEDLINE - Academic</collection><jtitle>Bioconjugate chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Drake, Richard R.</au><au>Slama, James T.</au><au>Wall, Katherine A.</au><au>Abramova, Margaret</au><au>D'Souza, Crislyn</au><au>Elbein, Alan D.</au><au>Crocker, Peter J.</au><au>Watt, David S.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Application of an N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine-substituted peptide as a heterobifunctional cross-linking agent in a study of protein O-glycosylation in yeast</atitle><jtitle>Bioconjugate chemistry</jtitle><addtitle>Bioconjugate Chem</addtitle><date>1992-01-01</date><risdate>1992</risdate><volume>3</volume><issue>1</issue><spage>69</spage><epage>73</epage><pages>69-73</pages><issn>1043-1802</issn><eissn>1520-4812</eissn><abstract>In order to investigate the O-mannosyltransferase involved in the initial O-mannosylation of glycoproteins in Saccharomyces cerevisiae, a photoactive hexapeptide, [125I]-N-(4-azido-2,3,5,6-tetrafluorobenzoyl)-3-iodo-Tyr-Asn-Pro-T hr-Ser-Val ([125I]azidoTyr-peptide), was synthesized by solid-phase techniques using a new photoactive cross-linking reagent, N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine, and resin-bound Asn-Pro-Thr(tBu)-Ser(tBu)-Val. When this modified hexapeptide substrate was incubated with O-mannosyltransferase preparations, the hexapeptide was an acceptor of [14C]-mannose from dolichol phosphate-[14C]mannose. After partially purifying the O-mannosyltransferase and photolabeling these enzyme preparations with [125I]azidoTyr-peptide, a ca. 82-kDa protein was shown to be the only apparent photolabeled protein that was protected by unmodified hexapeptide. This ca. 82-kDa protein may be the catalytic subunit of the O-mannosyltransferase. The susceptibility of the N-(4-azido-2,3,5,6-tetrafluorobenzoyl) moiety to reducing agents in aqueous buffers was also examined.</abstract><cop>Washington, DC</cop><pub>American Chemical Society</pub><pmid>1616952</pmid><doi>10.1021/bc00013a011</doi><tpages>5</tpages></addata></record> |
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| identifier | ISSN: 1043-1802 |
| ispartof | Bioconjugate chemistry, 1992-01, Vol.3 (1), p.69-73 |
| issn | 1043-1802 1520-4812 |
| language | eng |
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| source | ACS Publications; MEDLINE |
| subjects | Amino Acid Sequence Analytical, structural and metabolic biochemistry Azides - chemistry Azides - metabolism Biological and medical sciences Cross-Linking Reagents Enzymes and enzyme inhibitors Fundamental and applied biological sciences. Psychology Fungal Proteins - metabolism Glycoproteins - metabolism Glycosylation Mannosyltransferases - metabolism Molecular Sequence Data Saccharomyces cerevisiae - metabolism Spectrophotometry, Ultraviolet Tyrosine - analogs & derivatives Tyrosine - chemistry Tyrosine - metabolism |
| title | Application of an N-(4-azido-2,3,5,6-tetrafluorobenzoyl)tyrosine-substituted peptide as a heterobifunctional cross-linking agent in a study of protein O-glycosylation in yeast |
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