Chloroplast destined precursor proteins bind to distinct areas on the organellar surface as
visualized by immunogold decoration. Binding seems to occur predominantly in regions …

Routing of cytosolically synthesized precursor proteins into chloroplasts is a specific process
which involves a multitude of soluble and membrane components. In this review we wil1 …

Isolated outer chloroplast envelope membranes were solubilized by digitonin and separated
on linear sucrose density gradients. A membrane complex was recovered from the gradients …

The transit peptide of the lumenal 33-kDa oxygen-evolving polypeptide (OEE1) is capable of
directing the import and targeting of the foreign protein dihydrofolate reductase (DHFR) to …

A large number of plastid localized proteins are post‐translationally imported as precursor
proteins from the cytosol into the organelle. Recognition and translocation is accomplished …

Chloroplast structure and function depends vitally on the import of nuclear coded and
cytosolically synthesized polypeptide constituents (de Boer and Weisbeek 1991). Proteins of …

Most proteins involved in plastid biogenesis are encoded by the nuclear genome. They are
synthesised in the cytosol and have to be transported toward and subsequently translocated …

Most chloroplastic proteins are encoded in the nucleus, synthesized on cytosolic ribosomes
and subsequently imported into the organelle. In general, proteins destined for the …

The chloroplast inner envelope membrane contains many integral proteins which differ in
the number of α-helices that anchor the protein into the bilayer. For most of these proteins it …

Isolated outer envelope membrane from pea (Pisum sativum L.) chloroplasts can be used in
vitro to study binding and partial translocation of precursor proteins destined for the inside of …