Cookies Policy

This site uses cookies. By continuing to browse the site you are agreeing to our use of cookies.

I accept this policy

Find out more here


No metrics data to plot.
The attempt to load metrics for this article has failed.
The attempt to plot a graph for these metrics has failed.
The full text of this article is not currently available.

Brill’s MyBook program is exclusively available on BrillOnline Books and Journals. Students and scholars affiliated with an institution that has purchased a Brill E-Book on the BrillOnline platform automatically have access to the MyBook option for the title(s) acquired by the Library. Brill MyBook is a print-on-demand paperback copy which is sold at a favorably uniform low price.

Access this article

+ Tax (if applicable)
Add to Favorites
You must be logged in to use this functionality

image of Israel Journal of Plant Sciences

Many proteins found in the chloroplast are synthesized in the cytoplasm as transit peptide-containing precursor molecules. Stroma-targeted proteins have to cross the two envelope membranes; lumen proteins, however, have also to be transferred over the thylakoid membrane, i.e., they have to cross three biological membranes in order to reach their final location. Recent evidence shows that the routing of plastocyanin (PC) towards the lumen involves two post-translational transport processes and is mediated by two different regions of the transit peptide. Concomitant with the transport, the transit peptide is removed in two successive steps. The transit peptide consists of two functionally different domains. In this study we examine to what extent each domain is involved in import and routing and how far these two processes are linked. The results show that the N-terminal part of the transit peptide is responsible for import into the chloroplast. The N-terminal 43 amino acids are sufficient to direct other proteins into the stroma. The C-terminal part of the transit peptide is a prerequisite for routing inside the chloroplast but not for import. Transgenic tomato plants that constitutively express a foreign PC gene were used to study protein transport into different tissues. We conclude from these experiments that plastids of developmentally different tissues are capable of importing precursor proteins normally not found in these tissues. Most likely such plastids, though functionally and morphologically differentiated, have similar or identical protein import mechanisms when compared to the chloroplasts in green tissue. It is postulated that this transport mechanism evolved by the addition of a chloroplast-specific targeting peptide to the signal peptide-containing PC precursor of the endosymbiont, after the genetic information for this thylakoid protein had been transferred from the endosymbiont to the nucleus.

Affiliations: 1: Department of Molecular Cell Biology, Institute of Molecular Biology, University of Utrecht


Full text loading...


Data & Media loading...

Article metrics loading...



Can't access your account?
  • Tools

  • Add to Favorites
  • Printable version
  • Email this page
  • Subscribe to ToC alert
  • Get permissions
  • Recommend to your library

    You must fill out fields marked with: *

    Librarian details
    Your details
    Why are you recommending this title?
    Select reason:
    Israel Journal of Plant Sciences — Recommend this title to your library
  • Export citations
  • Key

  • Full access
  • Open Access
  • Partial/No accessInformation