Publication Date:
1993-02-05
Description:
Recoverin, a calcium ion (Ca2+)-binding protein of vertebrate photoreceptors, binds to photoreceptor membranes when the Ca2+ concentration is greater than 1 micromolar. This interaction requires a fatty acyl residue covalently linked to the recoverin amino (NH2)-terminus. Removal of the acyl residue, either by proteolytic cleavage of the NH2-terminus or by production of nonacylated recoverin, prevented recoverin from binding to membranes. The acylated recoverin NH2-terminus could be cleaved by trypsin only when Ca2+ was bound to recoverin. These results suggest that the hydrophobic NH2-terminus is constrained in Ca(2+)-free recoverin and liberated by Ca2+ binding. The hydrophobic acyl moiety of recoverin may interact with the membrane only when recoverin binds Ca2+.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Dizhoor, A M -- Chen, C K -- Olshevskaya, E -- Sinelnikova, V V -- Phillipov, P -- Hurley, J B -- EYO6641/EY/NEI NIH HHS/ -- New York, N.Y. -- Science. 1993 Feb 5;259(5096):829-32.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Department of Biochemistry, University of Washington, Seattle 98195.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/8430337" target="_blank"〉PubMed〈/a〉
Keywords:
1,2-Dipalmitoylphosphatidylcholine
;
Acylation
;
Animals
;
Antigens, Neoplasm/isolation & purification/*metabolism
;
Calcium/*metabolism/pharmacology
;
Calcium-Binding Proteins/isolation & purification/*metabolism
;
Cattle
;
Cell Membrane/metabolism
;
Egtazic Acid/pharmacology
;
Electrophoresis, Polyacrylamide Gel
;
*Eye Proteins
;
Hippocalcin
;
Kinetics
;
*Lipoproteins
;
Liposomes
;
Membrane Proteins/isolation & purification/*metabolism
;
Molecular Weight
;
Myristic Acid
;
Myristic Acids/*metabolism
;
*Nerve Tissue Proteins
;
Peptide Fragments/isolation & purification
;
Phosphatidylserines
;
Protein Binding
;
Recoverin
;
Rod Cell Outer Segment/*metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
