JCB logo
Avanti Polar Lipids, Inc.
  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents

This Article
Right arrow Full Text
Right arrow Full Text (PDF, 632K)
Right arrow PPT slides of all figures
Right arrow Alert me when this article is cited
Right arrow Citation Map
Services
Right arrow Email this article
Right arrow Similar articles in this journal
Right arrow Alert me to new content in the JCB
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Akita, M.
Right arrow Articles by Keegstra, K.
Right arrow Search for Related Content
PubMed
Right arrow Articles by Akita, M.
Right arrow Articles by Keegstra, K.
Social Bookmarking
 Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Facebook   Add to Reddit   Add to Technorati   Add to Twitter  
What's this?

© The Rockefeller University Press, 0021-9525/1997//983 $5.00
The Journal of Cell Biology, Volume 136, Number 5, , 1997 983-994


Article

Identification of Protein Transport Complexes in the Chloroplastic Envelope Membranes via Chemical Cross-Linking



Mitsuru Akita, Erik Nielsen, and Kenneth Keegstra

MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, Michigan 48824-1312

Transport of cytoplasmically synthesized proteins into chloroplasts uses an import machinery present in the envelope membranes. To identify the components of this machinery and to begin to examine how these components interact during transport, chemical cross-linking was performed on intact chloroplasts containing precursor proteins trapped at a particular stage of transport by ATP limitation. Large crosslinked complexes were observed using three different reversible homobifunctional cross-linkers. Three outer envelope membrane proteins (OEP86, OEP75, and OEP34) and one inner envelope membrane protein (IEP110), previously reported to be involved in protein import, were identified as components of these complexes. In addition to these membrane proteins, a stromal member of the hsp100 family, ClpC, was also present in the complexes. We propose that ClpC functions as a molecular chaperone, cooperating with other components to accomplish the transport of precursor proteins into chloroplasts. We also propose that each envelope membrane contains distinct translocation complexes and that a portion of these interact to form contact sites even in the absence of precursor proteins.


Abbreviations used in this paper: DSP, dithiobissuccinimidylpropionate; DST, disuccinimidyltartarate; DTSSP, dithiobissulfosuccinimidylpropionate; IEP and OEP, inner and outer envelope membrane proteins; LDS, lithiumdodecylsulfate; LS, the large subunit of ribulose 1,5-bisphosphate carboxylase; prSS, precursor to the small subunit of ribulose 1,5-bisphosphate carboxylase; Rubisco, ribulose 1,5-bisphosphate carboxylase; S78, stromal hsp70; SS, mature small subunit.

Address all correspondence to Kenneth Keegstra, MSU-DOE Plant Research Laboratory, Michigan State University, East Lansing, MI 48824-1312. Tel.: (517) 353-7874. Fax: (517) 353-9168. E-mail: Keegstra{at}msu.edu



Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Facebook Facebook   Add to Reddit Reddit   Add to Technorati Technorati   Add to Twitter Twitter    What's this?


This article has been cited by other articles:



  Home | Help | Feedback | Subscriptions | Archive | Search | Table of Contents