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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Bibliographic Details
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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Summary: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.
ISSN:0006-2960
1520-4995
DOI:10.1021/bi00069a036