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. 1990 Aug;87(15):5778–5782. doi: 10.1073/pnas.87.15.5778

Sequence analysis and protein import studies of an outer chloroplast envelope polypeptide.

M Salomon 1, K Fischer 1, U I Flügge 1, J Soll 1
PMCID: PMC54411  PMID: 2377616

Abstract

A chloroplast outer envelope membrane protein was cloned and sequenced and from the sequence it was possible to deduce a polypeptide of 6.7 kDa. It has only one membrane-spanning region; the C terminus extends into the cytosol, whereas the N terminus is exposed to the space between the two envelope membranes. The protein was synthesized in an in vitro transcription-translation system to study its routing into isolated chloroplasts. The import studies revealed that the 6.7-kDa protein followed a different and heretofore undescribed translocation pathway in the respect that (i) it does not have a cleavable transit sequence, (ii) it does not require ATP hydrolysis for import, and (iii) protease-sensitive components that are responsible for recognition of precursor proteins destined for the inside of the chloroplasts are not involved in routing the 6.7-kDa polypeptide to the outer chloroplast envelope.

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