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The outer plastid envelope protein Oep16: role as precursor translocase in import of protochlorophyllide oxidoreductase A.


ABSTRACT: A 16-kDa plastid envelope protein was identified by chemical crosslinking that interacts with the precursor of NADPH:protochlorophyllide oxdidoreductase A (pPORA) during its posttranslational import into isolated barley chloroplasts. Protein purification and subsequent protein sequencing showed that the 16-kDa protein is an ortholog of a previously identified outer plastid envelope protein, Oep16. A protein of identical size was present in barley etioplasts and interacted with pPORA. Similar 16-kDa protein-dependent crosslink products of pPORA were detected in wheat, pea, and Arabidopsis chloroplasts. Database analyses revealed that the 16-kDa protein belongs to a family of preprotein and amino acid transporters found in free-living bacteria and endosymbiotic mitochondria and chloroplasts. Antibodies raised against the 16-kDa protein inhibited import of pPORA, highlighting its role in protein import.

SUBMITTER: Reinbothe S 

PROVIDER: S-EPMC357075 | biostudies-literature | 2004 Feb

REPOSITORIES: biostudies-literature

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The outer plastid envelope protein Oep16: role as precursor translocase in import of protochlorophyllide oxidoreductase A.

Reinbothe Steffen S   Quigley Françoise F   Springer Armin A   Schemenewitz Andreas A   Reinbothe Christiane C  

Proceedings of the National Academy of Sciences of the United States of America 20040209 7


A 16-kDa plastid envelope protein was identified by chemical crosslinking that interacts with the precursor of NADPH:protochlorophyllide oxdidoreductase A (pPORA) during its posttranslational import into isolated barley chloroplasts. Protein purification and subsequent protein sequencing showed that the 16-kDa protein is an ortholog of a previously identified outer plastid envelope protein, Oep16. A protein of identical size was present in barley etioplasts and interacted with pPORA. Similar 16-  ...[more]

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