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Phosphorylation sites in bovine rhodopsin

Bovine rhodopsin has been phosphorylated in rod outer segments by ATP and endogenous rhodopsin kinase. Mono-, di-, and triphosphorylated rhodopsins have been prepared by chromatofocusing. Nearly all of the phosphate is found in peptide 330-348, formed by digestion of phosphorhodopsins with endoprote...

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Published in:	Biochemistry (Easton) 1993-05, Vol.32 (18), p.4968-4974
Main Authors:	McDowell, J. Hugh, Nawrocki, Joseph P, Hargrave, Paul A
Format:	Article
Language:	English
Subjects:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Fundamental and applied biological sciences. Psychology Non metallic chromoproteins, photoproteins Phosphopeptides - isolation & purification Phosphopeptides - metabolism Phosphoproteins - isolation & purification Phosphoproteins - metabolism Phosphorylation Phosphoserine - metabolism Phosphothreonine - metabolism Protein Processing, Post-Translational Proteins Rhodopsin - isolation & purification Rhodopsin - metabolism Rod Cell Outer Segment - metabolism Sequence Analysis
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cited_by	cdi_FETCH-LOGICAL-a383t-fbdf19f92af6d1d1d1bf20c7625a44c22eebe17d28d8da687898b0cf92e531843
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container_end_page	4974
container_issue	18
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container_title	Biochemistry (Easton)
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creator	McDowell, J. Hugh Nawrocki, Joseph P Hargrave, Paul A
description	Bovine rhodopsin has been phosphorylated in rod outer segments by ATP and endogenous rhodopsin kinase. Mono-, di-, and triphosphorylated rhodopsins have been prepared by chromatofocusing. Nearly all of the phosphate is found in peptide 330-348, formed by digestion of phosphorhodopsins with endoproteinase Asp-N. Sequence analysis of the phosphopeptides shows that monophosphorylated rhodopsin consists of a mixture containing rhodopsins phosphorylated at 338Ser and 343Ser. Diphosphorylated rhodopsin is phosphorylated at both 338Ser and 343Ser. When rhodopsin becomes triphosphorylated it does not become phosphorylated on 334Ser but appears to become phosphorylated on one or more of the four threonine residues: 335Thr, 336Thr, 340Thr, and 342Thr.
doi_str_mv	10.1021/bi00069a036
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When rhodopsin becomes triphosphorylated it does not become phosphorylated on 334Ser but appears to become phosphorylated on one or more of the four threonine residues: 335Thr, 336Thr, 340Thr, and 342Thr.</description><identifier>ISSN: 0006-2960</identifier><identifier>EISSN: 1520-4995</identifier><identifier>DOI: 10.1021/bi00069a036</identifier><identifier>PMID: 8490033</identifier><language>eng</language><publisher>Washington, DC: American Chemical Society</publisher><subject>Analytical, structural and metabolic biochemistry ; Animals ; Biological and medical sciences ; Cattle ; Fundamental and applied biological sciences. Psychology ; Non metallic chromoproteins, photoproteins ; Phosphopeptides - isolation & purification ; Phosphopeptides - metabolism ; Phosphoproteins - isolation & purification ; Phosphoproteins - metabolism ; Phosphorylation ; Phosphoserine - metabolism ; Phosphothreonine - metabolism ; Protein Processing, Post-Translational ; Proteins ; Rhodopsin - isolation & purification ; Rhodopsin - metabolism ; Rod Cell Outer Segment - metabolism ; Sequence Analysis</subject><ispartof>Biochemistry (Easton), 1993-05, Vol.32 (18), p.4968-4974</ispartof><rights>1993 INIST-CNRS</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-a383t-fbdf19f92af6d1d1d1bf20c7625a44c22eebe17d28d8da687898b0cf92e531843</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/bi00069a036$$EPDF$$P50$$Gacs$$H</linktopdf><linktohtml>$$Uhttps://pubs.acs.org/doi/10.1021/bi00069a036$$EHTML$$P50$$Gacs$$H</linktohtml><link.rule.ids>314,780,784,27064,27924,27925,56766,56816</link.rule.ids><backlink>$$Uhttp://pascal-francis.inist.fr/vibad/index.php?action=getRecordDetail&idt=4779333$$DView record in Pascal Francis$$Hfree_for_read</backlink><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/8490033$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>McDowell, J. Hugh</creatorcontrib><creatorcontrib>Nawrocki, Joseph P</creatorcontrib><creatorcontrib>Hargrave, Paul A</creatorcontrib><title>Phosphorylation sites in bovine rhodopsin</title><title>Biochemistry (Easton)</title><addtitle>Biochemistry</addtitle><description>Bovine rhodopsin has been phosphorylated in rod outer segments by ATP and endogenous rhodopsin kinase. Mono-, di-, and triphosphorylated rhodopsins have been prepared by chromatofocusing. Nearly all of the phosphate is found in peptide 330-348, formed by digestion of phosphorhodopsins with endoproteinase Asp-N. Sequence analysis of the phosphopeptides shows that monophosphorylated rhodopsin consists of a mixture containing rhodopsins phosphorylated at 338Ser and 343Ser. Diphosphorylated rhodopsin is phosphorylated at both 338Ser and 343Ser. When rhodopsin becomes triphosphorylated it does not become phosphorylated on 334Ser but appears to become phosphorylated on one or more of the four threonine residues: 335Thr, 336Thr, 340Thr, and 342Thr.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cattle</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Non metallic chromoproteins, photoproteins</subject><subject>Phosphopeptides - isolation & purification</subject><subject>Phosphopeptides - metabolism</subject><subject>Phosphoproteins - isolation & purification</subject><subject>Phosphoproteins - metabolism</subject><subject>Phosphorylation</subject><subject>Phosphoserine - metabolism</subject><subject>Phosphothreonine - metabolism</subject><subject>Protein Processing, Post-Translational</subject><subject>Proteins</subject><subject>Rhodopsin - isolation & purification</subject><subject>Rhodopsin - metabolism</subject><subject>Rod Cell Outer Segment - metabolism</subject><subject>Sequence Analysis</subject><issn>0006-2960</issn><issn>1520-4995</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1993</creationdate><recordtype>article</recordtype><recordid>eNpt0M1LwzAYBvAgypzTk2ehB1FEqvlo83GUoVPwY7B5DmmbsMyumUkr7r-3s2V4kBxC8vzyEh4AThG8QRCj28xCCKlQkNA9MEQphnEiRLoPhtv7GAsKD8FRCMv2mECWDMCAJwJCQobgarpwYb1wflOq2roqCrbWIbJVlLkvW-nIL1zh1sFWx-DAqDLok34fgfeH-_n4MX5-mzyN755jRTipY5MVBgkjsDK0QNuVGQxzRnGqkiTHWOtMI1ZgXvBCUc644BnM2wc6JYgnZAQuurlr7z4bHWq5siHXZakq7ZogWcoIxZS38LqDuXcheG3k2tuV8huJoNwWI_8U0-qzfmyTrXSxs30TbX7e5yrkqjReVbkNO5YwJsgviztmQ62_d7HyH5IywlI5n87khMPXWUqhfGn9ZedVHuTSNb5qu_v3gz9CrIUl</recordid><startdate>19930511</startdate><enddate>19930511</enddate><creator>McDowell, J. 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Psychology</topic><topic>Non metallic chromoproteins, photoproteins</topic><topic>Phosphopeptides - isolation & purification</topic><topic>Phosphopeptides - metabolism</topic><topic>Phosphoproteins - isolation & purification</topic><topic>Phosphoproteins - metabolism</topic><topic>Phosphorylation</topic><topic>Phosphoserine - metabolism</topic><topic>Phosphothreonine - metabolism</topic><topic>Protein Processing, Post-Translational</topic><topic>Proteins</topic><topic>Rhodopsin - isolation & purification</topic><topic>Rhodopsin - metabolism</topic><topic>Rod Cell Outer Segment - metabolism</topic><topic>Sequence Analysis</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>McDowell, J. Hugh</creatorcontrib><creatorcontrib>Nawrocki, Joseph P</creatorcontrib><creatorcontrib>Hargrave, Paul A</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>Biochemistry (Easton)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>McDowell, J. 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subjects	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cattle Fundamental and applied biological sciences. Psychology Non metallic chromoproteins, photoproteins Phosphopeptides - isolation & purification Phosphopeptides - metabolism Phosphoproteins - isolation & purification Phosphoproteins - metabolism Phosphorylation Phosphoserine - metabolism Phosphothreonine - metabolism Protein Processing, Post-Translational Proteins Rhodopsin - isolation & purification Rhodopsin - metabolism Rod Cell Outer Segment - metabolism Sequence Analysis
title	Phosphorylation sites in bovine rhodopsin
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