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Science 11 November 1994: Vol. 266. no. 5187, pp. 1007 - 1012 DOI: 10.1126/science.7973649
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Articles
Science, Vol 266, Issue 5187, 1007-1012
Copyright © 1994 by American Association for the Advancement of Science
Isolation of components of the chloroplast protein import machinery
DJ Schnell,
F Kessler,
and
G Blobel
Department of Biological Sciences, Rutgers, State University of New Jersey, Newark 07102.
Components of the protein import machinery of the chloroplast were isolated by a procedure in which the import machinery was engaged in vitro with a tagged import substrate under conditions that yielded largely chloroplast envelope-bound import intermediates. Subsequent detergent solubilization of envelope membranes showed that six envelope polypeptides copurified specifically and, apparently, stoichiometrically with the import intermediates. Four of these polypeptides are components of the outer membrane import machinery and are associated with early import intermediates. Two of these polypeptides have been characterized. One is a homolog of the heat shock protein hsp70; the other one is a channel-protein candidate.
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- S. Reinbothe, R. Mache, and C. Reinbothe (2000)
PNAS
97, 9795-9800
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- In Vivo Analysis of the Role of atTic20 in Protein Import into Chloroplasts.
- X. Chen, M. D. Smith, L. Fitzpatrick, and D. J. Schnell (2002)
PLANT CELL
14, 641-654
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