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Science 23 December 1994: Vol. 266. no. 5193, pp. 1989 - 1992 DOI: 10.1126/science.7801125
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Articles
Science, Vol 266, Issue 5193, 1989-1992
Copyright © 1994 by American Association for the Advancement of Science
A receptor component of the chloroplast protein translocation machinery
S Hirsch,
E Muckel,
F Heemeyer,
G von Heijne,
and
J Soll
Botanisches Institut, Universitat Kiel, Germany.
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.
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139, 1677-1685
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272, 18725-18731
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- H.-m. Li and L.-J. Chen (1997)
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272, 10968-10974
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- A. Kouranov and D. J. Schnell (1996)
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271, 31009-31012
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- Phosphorylation of the Transit Sequence of Chloroplast Precursor Proteins.
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271, 6545-6554
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271, 4082-4085
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- Isolation and Characterization of a cDNA Clone Encoding a Member of the Com44/Cim44 Envelope Components of the Chloroplast Protein Import Apparatus.
- K. Ko, D. Budd, C. Wu, F. Seibert, L. Kourtz, and Z. W. Ko (1995)
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270, 28601-28608
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- Toc34 is a preprotein receptor regulated by GTP and phosphorylation.
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PNAS
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