A bipartite chromatophore transit peptide and N-terminal protein processing in the Paulinella chromatophore.


Journal

Plant physiology
ISSN: 1532-2548
Titre abrégé: Plant Physiol
Pays: United States
ID NLM: 0401224

Informations de publication

Date de publication:
03 05 2022
Historique:
received: 19 09 2021
accepted: 06 12 2021
pubmed: 20 1 2022
medline: 10 5 2022
entrez: 19 1 2022
Statut: ppublish

Résumé

The amoeba Paulinella chromatophora contains photosynthetic organelles, termed chromatophores, which evolved independently from plastids in plants and algae. At least one-third of the chromatophore proteome consists of nucleus-encoded (NE) proteins that are imported across the chromatophore double envelope membranes. Chromatophore-targeted proteins exceeding 250 amino acids (aa) carry a conserved N-terminal extension presumably involved in protein targeting, termed the chromatophore transit peptide (crTP). Short imported proteins do not carry discernable targeting signals. To explore whether the import of proteins is accompanied by their N-terminal processing, here we identified N-termini of 208 chromatophore-localized proteins by a mass spectrometry-based approach. Our study revealed extensive N-terminal acetylation and proteolytic processing in both NE and chromatophore-encoded (CE) fractions of the chromatophore proteome. Mature N-termini of 37 crTP-carrying proteins were identified, of which 30 were cleaved in a common processing region. Surprisingly, only the N-terminal ∼50 aa (part 1) become cleaved upon import. This part contains a conserved adaptor protein-1 complex-binding motif known to mediate protein sorting at the trans-Golgi network followed by a predicted transmembrane helix, implying that part 1 anchors the protein co-translationally in the endoplasmic reticulum and mediates trafficking to the chromatophore via the Golgi. The C-terminal part 2 contains conserved secondary structural elements, remains attached to the mature proteins, and might mediate translocation across the chromatophore inner membrane. Short imported proteins remain largely unprocessed. Finally, this work illuminates N-terminal processing of proteins encoded in an evolutionary-early-stage organelle and suggests host-derived posttranslationally acting factors involved in regulation of the CE chromatophore proteome.

Identifiants

pubmed: 35043947
pii: 6511448
doi: 10.1093/plphys/kiac012
pmc: PMC9070848
doi:

Substances chimiques

Peptides 0
Proteome 0

Types de publication

Journal Article

Langues

eng

Sous-ensembles de citation

IM

Pagination

152-164

Informations de copyright

© American Society of Plant Biologists 2022. All rights reserved. For permissions, please email: journals.permissions@oup.com.

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Auteurs

Linda Oberleitner (L)

Department of Biology, Institute of Microbial Cell Biology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.

Andreas Perrar (A)

Central Institute for Engineering, Electronics and Analytics, ZEA-3, Forschungszentrum Jülich, 52425 Jülich, Germany.
Cologne Excellence Cluster on Stress Responses in Ageing-Associated Diseases, CECAD, Medical Faculty and University Hospital, University of Cologne, 50931 Cologne, Germany.

Luis Macorano (L)

Department of Biology, Institute of Microbial Cell Biology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.

Pitter F Huesgen (PF)

Central Institute for Engineering, Electronics and Analytics, ZEA-3, Forschungszentrum Jülich, 52425 Jülich, Germany.
Cologne Excellence Cluster on Stress Responses in Ageing-Associated Diseases, CECAD, Medical Faculty and University Hospital, University of Cologne, 50931 Cologne, Germany.
Department of Chemistry, Institute of Biochemistry, University of Cologne, 50674 Cologne, Germany.

Eva C M Nowack (ECM)

Department of Biology, Institute of Microbial Cell Biology, Heinrich Heine University Düsseldorf, 40225 Düsseldorf, Germany.

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