Details
| Originalsprache | Englisch |
|---|---|
| Seiten (von - bis) | 1345-1362 |
| Seitenumfang | 18 |
| Fachzeitschrift | Molecular and Cellular Proteomics |
| Jahrgang | 18 |
| Ausgabenummer | 7 |
| Frühes Online-Datum | 25 Apr. 2019 |
| Publikationsstatus | Veröffentlicht - Juli 2019 |
Abstract
Mitochondrial transcripts are subject to a wealth of processing mechanisms including cis- and trans-splicing events, as well as base modifications (RNA editing). HUndreds of proteins are required for these processes in plant mitochondria, many of which belong to the pentatricopeptide repeat (PPR) protein superfamily. The structure, localization, and function of these proteins is only poorly Understood. Here we present evidence that several PPR proteins are boUnd to mitoribosomes in plants. A novel complexome profiling strategy in combination with chemical crosslinking has been employed to systematically define the protein constituents of the large and the small ribosomal subunits in the mitochondria of plants. We identified more than 80 ribosomal proteins, which include several PPR proteins and other non-conventional ribosomal proteins. These findings reveal a potential coupling of transcriptional and translational events in the mitochondria of plants. Furthermore, the data indicate an extremely high molecular mass of the “small” subunit, even exceeding that of the “large” subunit.
ASJC Scopus Sachgebiete
- Chemie (insg.)
- Analytische Chemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Biochemie
- Biochemie, Genetik und Molekularbiologie (insg.)
- Molekularbiologie
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in: Molecular and Cellular Proteomics, Jahrgang 18, Nr. 7, 07.2019, S. 1345-1362.
Publikation: Beitrag in Fachzeitschrift › Artikel › Forschung › Peer-Review
}
TY - JOUR
T1 - Complexome Profiling Reveals Association of PPR Proteins with Ribosomes in the Mitochondria of Plants
AU - Rugen, Nils
AU - Straube, Henryk
AU - Franken, Linda E.
AU - Braun, Hans Peter
AU - Eubel, Holger
N1 - Funding information: ?S This article contains supplemental material. § To whom correspondence should be addressed. E-mail: heubel@genetik.uni-hannover.de. ¶ The research described in this manuscript was supported by the Deutsche Forschungsgemeinschaft (DFG, grant EU 54/4). This work was in part made possible by an EMBO long-term fellowship (ALTF 356–2018) awarded to Linda Franken.
PY - 2019/7
Y1 - 2019/7
N2 - Mitochondrial transcripts are subject to a wealth of processing mechanisms including cis- and trans-splicing events, as well as base modifications (RNA editing). HUndreds of proteins are required for these processes in plant mitochondria, many of which belong to the pentatricopeptide repeat (PPR) protein superfamily. The structure, localization, and function of these proteins is only poorly Understood. Here we present evidence that several PPR proteins are boUnd to mitoribosomes in plants. A novel complexome profiling strategy in combination with chemical crosslinking has been employed to systematically define the protein constituents of the large and the small ribosomal subunits in the mitochondria of plants. We identified more than 80 ribosomal proteins, which include several PPR proteins and other non-conventional ribosomal proteins. These findings reveal a potential coupling of transcriptional and translational events in the mitochondria of plants. Furthermore, the data indicate an extremely high molecular mass of the “small” subunit, even exceeding that of the “large” subunit.
AB - Mitochondrial transcripts are subject to a wealth of processing mechanisms including cis- and trans-splicing events, as well as base modifications (RNA editing). HUndreds of proteins are required for these processes in plant mitochondria, many of which belong to the pentatricopeptide repeat (PPR) protein superfamily. The structure, localization, and function of these proteins is only poorly Understood. Here we present evidence that several PPR proteins are boUnd to mitoribosomes in plants. A novel complexome profiling strategy in combination with chemical crosslinking has been employed to systematically define the protein constituents of the large and the small ribosomal subunits in the mitochondria of plants. We identified more than 80 ribosomal proteins, which include several PPR proteins and other non-conventional ribosomal proteins. These findings reveal a potential coupling of transcriptional and translational events in the mitochondria of plants. Furthermore, the data indicate an extremely high molecular mass of the “small” subunit, even exceeding that of the “large” subunit.
UR - http://www.scopus.com/inward/record.url?scp=85070954690&partnerID=8YFLogxK
U2 - 10.1074/mcp.RA119.001396
DO - 10.1074/mcp.RA119.001396
M3 - Article
C2 - 31023727
AN - SCOPUS:85068688260
VL - 18
SP - 1345
EP - 1362
JO - Molecular and Cellular Proteomics
JF - Molecular and Cellular Proteomics
SN - 1535-9476
IS - 7
ER -