Publication Date:
1994-12-23
Description:
The chloroplast outer envelope protein OEP86 functions as a receptor in precursor protein translocation into chloroplasts. Sequence analysis suggests that the precursor of OEP86 is directed to the chloroplast outer envelope by a cleavable, negatively charged, and unusually long amino-terminal peptide. This presequence is unlike other potential targeting signals and suggests the existence of another membrane insertion pathway. Insertion of precursor OEP86 required the hydrolysis of adenosine triphosphate and the existence of surface exposed chloroplast membrane components, and it was not competed by another precursor protein destined for the internal plastid compartments.〈br /〉〈span class="detail_caption"〉Notes: 〈/span〉Hirsch, S -- Muckel, E -- Heemeyer, F -- von Heijne, G -- Soll, J -- New York, N.Y. -- Science. 1994 Dec 23;266(5193):1989-92.〈br /〉〈span class="detail_caption"〉Author address: 〈/span〉Botanisches Institut, Universitat Kiel, Germany.〈br /〉〈span class="detail_caption"〉Record origin:〈/span〉 〈a href="http://www.ncbi.nlm.nih.gov/pubmed/7801125" target="_blank"〉PubMed〈/a〉
Keywords:
Adenosine Triphosphate/metabolism
;
Amino Acid Sequence
;
Chloroplast Proteins
;
Chloroplasts/*metabolism
;
*GTP-Binding Proteins
;
Hydrogen-Ion Concentration
;
Intracellular Membranes/metabolism
;
Molecular Sequence Data
;
Molecular Weight
;
Peas
;
Plant Proteins/chemistry/*metabolism
;
Protein Precursors/chemistry/*metabolism
;
Protein Processing, Post-Translational
;
Ribulose-Bisphosphate Carboxylase/metabolism
Print ISSN:
0036-8075
Electronic ISSN:
1095-9203
Topics:
Biology
,
Chemistry and Pharmacology
,
Computer Science
,
Medicine
,
Natural Sciences in General
,
Physics
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