Structure of the multi-subunit chloroplast RNA polymerase

verfasst von: Paula F V do Prado, Frederik M Ahrens, Monique Liebers, Noah Ditz, Hans-Peter Braun, Thomas Pfannschmidt, Hauke Hillen
Abstract: Chloroplasts contain a dedicated genome that encodes subunits of the photosynthesis machinery. Transcription of photosynthesis genes is predominantly carried out by a plastid-encoded RNA polymerase (PEP), a nearly 1 MDa complex composed of core subunits with homology to eubacterial RNA polymerases (RNAPs) and at least 12 additional chloroplast-specific PEP-associated proteins (PAPs). However, the architecture of this complex and the functions of the PAPs remain unknown. Here, we report the cryo-EM structure of a 19-subunit PEP complex from Sinapis alba (white mustard). The structure reveals that the PEP core resembles prokaryotic and nuclear RNAPs but contains chloroplast-specific features that mediate interactions with the PAPs. The PAPs are unrelated to known transcription factors and arrange around the core in a unique fashion. Their structures suggest potential functions during transcription in the chemical environment of chloroplasts. These results reveal structural insights into chloroplast transcription and provide a framework for understanding photosynthesis gene expression.
Organisationseinheit(en): Institut für Botanik
AG Pflanzenphysiologie
Institut für Pflanzengenetik
Abteilung Pflanzenmolekularbiologie und Pflanzenproteomik
Externe Organisation(en): Georg-August-Universität Göttingen
Universitätsmedizin Göttingen (UMG)
Typ: Artikel
Journal: Molecular cell
Band: 84
Seiten: 910-925.e5
ISSN: 1097-2765
Publikationsdatum: 07.03.2024
Publikationsstatus: Veröffentlicht
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Molekularbiologie, Zellbiologie
Elektronische Version(en): https://doi.org/10.1016/j.molcel.2024.02.003 (Zugang: Offen)

BibTeX

@article{0e96dc8f0ca9484c8f5ab7234791e72b,
title = "Structure of the multi-subunit chloroplast RNA polymerase",
abstract = "Chloroplasts contain a dedicated genome that encodes subunits of the photosynthesis machinery. Transcription of photosynthesis genes is predominantly carried out by a plastid-encoded RNA polymerase (PEP), a nearly 1 MDa complex composed of core subunits with homology to eubacterial RNA polymerases (RNAPs) and at least 12 additional chloroplast-specific PEP-associated proteins (PAPs). However, the architecture of this complex and the functions of the PAPs remain unknown. Here, we report the cryo-EM structure of a 19-subunit PEP complex from Sinapis alba (white mustard). The structure reveals that the PEP core resembles prokaryotic and nuclear RNAPs but contains chloroplast-specific features that mediate interactions with the PAPs. The PAPs are unrelated to known transcription factors and arrange around the core in a unique fashion. Their structures suggest potential functions during transcription in the chemical environment of chloroplasts. These results reveal structural insights into chloroplast transcription and provide a framework for understanding photosynthesis gene expression.",
keywords = "chloroplast, cryo-EM, gene expression, organelle, photosynthesis, plastid, RNA, RNA polymerase, structural biology, transcription",
author = "{do Prado}, {Paula F V} and Ahrens, {Frederik M} and Monique Liebers and Noah Ditz and Hans-Peter Braun and Thomas Pfannschmidt and Hauke Hillen",
note = "We thank Christian Dienemann and Ulrich Steuerwald (MPI-NAT cryo-EM facility) for technical assistance. This work was funded by the Deutsche Forschungsgemeinschaft under Germany's Excellence Strategy EXC 2067/1-390729940 (H.S.H.), Hertha Sponer College (P.F.V.d.P.), FOR2848 (P10, H.S.H.), SFB1565 (project number 469281184, P13, H.S.H.), PF323-7 (T.P.), the framework of the Priority Programme {"}MAdLand - Molecular Adaption to Land: Plant Evolution to Change (SPP2237, T.P.), PF323-9 (T.P.), and by the European Union (ERC Starting Grant MitoRNA, grant agreement no. 101116869, to H.S.H.). Views and opinions expressed are those of the author(s) only and do not necessarily reflect those of the European Union or the European Research Council Executive Agency. Neither the European Union nor the granting authority can be held responsible for them.",
year = "2024",
month = mar,
day = "7",
doi = "10.1016/j.molcel.2024.02.003",
language = "English",
volume = "84",
pages = "910--925.e5",
journal = "Molecular cell",
issn = "1097-2765",
publisher = "Cell Press",
number = "5",
}