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Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids.


ABSTRACT: In organisms with complex plastids acquired by secondary endosymbiosis from a photosynthetic eukaryote, the majority of plastid proteins are nuclear-encoded, translated on cytoplasmic ribosomes, and guided across four membranes by a bipartite targeting sequence. In-depth understanding of this vital import process has been impeded by a lack of information about the transit peptide part of this sequence, which mediates transport across the inner three membranes. We determined the mature N-termini of hundreds of proteins from the model diatom Thalassiosira pseudonana, revealing extensive N-terminal modification by acetylation and proteolytic processing in both cytosol and plastid. We identified 63 mature N-termini of nucleus-encoded plastid proteins, deduced their complete transit peptide sequences, determined a consensus motif for their cleavage by the stromal processing peptidase, and found evidence for subsequent processing by a plastid methionine aminopeptidase. The cleavage motif differs from that of higher plants, but is shared with other eukaryotes with complex plastids.

SUBMITTER: Huesgen PF 

PROVIDER: S-EPMC3774753 | biostudies-literature | 2013

REPOSITORIES: biostudies-literature

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Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids.

Huesgen Pitter F PF   Alami Meriem M   Lange Philipp F PF   Foster Leonard J LJ   Schröder Wolfgang P WP   Schröder Wolfgang P WP   Overall Christopher M CM   Green Beverley R BR  

PloS one 20130916 9


In organisms with complex plastids acquired by secondary endosymbiosis from a photosynthetic eukaryote, the majority of plastid proteins are nuclear-encoded, translated on cytoplasmic ribosomes, and guided across four membranes by a bipartite targeting sequence. In-depth understanding of this vital import process has been impeded by a lack of information about the transit peptide part of this sequence, which mediates transport across the inner three membranes. We determined the mature N-termini  ...[more]

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