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PMID: 2377616 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't

Sequence analysis and protein import studies of an outer chloroplast envelope polypeptide.

Salomon M, Fischer K, Flügge UI, Soll J

Abstract

A chloroplast outer envelope membrane protein was cloned and sequenced and from the sequence it was possible to deduce a polypeptide of 6.7 kDa. It has only one membrane-spanning region; the C terminus extends into the cytosol, whereas the N terminus is exposed to the space between the two envelope membranes. The protein was synthesized in an in vitro transcription-translation system to study its routing into isolated chloroplasts. The import studies revealed that the 6.7-kDa protein followed a different and heretofore undescribed translocation pathway in the respect that (i) it does not have a cleavable transit sequence, (ii) it does not require ATP hydrolysis for import, and (iii) protease-sensitive components that are responsible for recognition of precursor proteins destined for the inside of the chloroplasts are not involved in routing the 6.7-kDa polypeptide to the outer chloroplast envelope.

MeSH Terms
Amino Acid Sequence Base Sequence Chloroplasts/metabolism Intracellular Membranes/metabolism Kinetics Membrane Proteins/genetics,metabolism Molecular Sequence Data Plants/genetics,metabolism Protein Biosynthesis Protein Conformation Protein Processing, Post-Translational Thermodynamics
Chemicals
Membrane Proteins
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Salomon M
Botanisches Institut, Universität Munich, Federal Republic of Germany.
Fischer K
Flügge U I
Soll J
References (28)
28 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
Published
1990-08-00
Pages
5778-82
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC54411
Subset
IM
Databases
GENBANK
M35665, M36587
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