outer plastid envelope protein Oep16: Role as precursor translocase in import of protochlorophyllide oxidoreductase A

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...

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Bibliographic Details
Published in:Proceedings of the National Academy of Sciences - PNAS 2004-02, Vol.101 (7), p.2203-2208
Main Authors: Reinbothe, S, Quigley, F, Springer, A, Schemenewitz, A, Reinbothe, C
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Antiserum
Arabidopsis
Barley
Biological Sciences
Botany
Chloroplast Proteins
Chloroplasts
Cross-Linking Reagents
Enzymes
Etioplasts
Evolution, Molecular
Hordeum vulgare
Imports
Intracellular Membranes - chemistry
Intracellular Membranes - metabolism
Ion Channels - chemistry
Ion Channels - metabolism
Membrane Transport Proteins - chemistry
Membrane Transport Proteins - metabolism
Molecular Sequence Data
Molecular Weight
Nucleic acid precursors
Oxidoreductases Acting on CH-CH Group Donors - metabolism
Peas
Plant Cells
Plant Proteins - chemistry
Plant Proteins - metabolism
Plants - chemistry
Plants - enzymology
Plants - metabolism
Plastids
Plastids - chemistry
Plastids - metabolism
Protein Binding
Protein precursors
Protein Precursors - chemistry
Protein Precursors - metabolism
Protein Transport
Proteins
Triticum aestivum
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Summary: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.
ISSN:0027-8424
1091-6490
DOI:10.1073/pnas.0301962101