Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids.
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...
| Main Authors: | , , , , , , |
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| Format: | Article |
| Language: | English |
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Public Library of Science (PLoS)
2013-01-01
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| Series: | PLoS ONE |
| Online Access: | http://europepmc.org/articles/PMC3774753?pdf=render |
| _version_ | 1828524801528954880 |
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| author | Pitter F Huesgen Meriem Alami Philipp F Lange Leonard J Foster Wolfgang P Schröder Christopher M Overall Beverley R Green |
| author_facet | Pitter F Huesgen Meriem Alami Philipp F Lange Leonard J Foster Wolfgang P Schröder Christopher M Overall Beverley R Green |
| author_sort | Pitter F Huesgen |
| collection | DOAJ |
| description | 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. |
| first_indexed | 2024-12-11T20:54:26Z |
| format | Article |
| id | doaj.art-05ab4fbc7e9c4efe9d68d2c6c83c8ab0 |
| institution | Directory Open Access Journal |
| issn | 1932-6203 |
| language | English |
| last_indexed | 2024-12-11T20:54:26Z |
| publishDate | 2013-01-01 |
| publisher | Public Library of Science (PLoS) |
| record_format | Article |
| series | PLoS ONE |
| spelling | doaj.art-05ab4fbc7e9c4efe9d68d2c6c83c8ab02022-12-22T00:51:08ZengPublic Library of Science (PLoS)PLoS ONE1932-62032013-01-0189e7448310.1371/journal.pone.0074483Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids.Pitter F HuesgenMeriem AlamiPhilipp F LangeLeonard J FosterWolfgang P SchröderChristopher M OverallBeverley R GreenIn 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.http://europepmc.org/articles/PMC3774753?pdf=render |
| spellingShingle | Pitter F Huesgen Meriem Alami Philipp F Lange Leonard J Foster Wolfgang P Schröder Christopher M Overall Beverley R Green Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. PLoS ONE |
| title | Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. |
| title_full | Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. |
| title_fullStr | Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. |
| title_full_unstemmed | Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. |
| title_short | Proteomic amino-termini profiling reveals targeting information for protein import into complex plastids. |
| title_sort | proteomic amino termini profiling reveals targeting information for protein import into complex plastids |
| url | http://europepmc.org/articles/PMC3774753?pdf=render |
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