Structure of the multi-subunit chloroplast RNA polymerase

Research output: Contribution to journalArticleResearchpeer review

Authors

  • Paula F V do Prado
  • Frederik M Ahrens
  • Monique Liebers
  • Noah Ditz
  • Hans-Peter Braun
  • Thomas Pfannschmidt
  • Hauke Hillen

External Research Organisations

  • University of Göttingen
  • Universitätsmedizin Göttingen (UMG)
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Details

Original languageEnglish
Pages (from-to)910-925.e5
JournalMolecular cell
Volume84
Issue number5
Early online date29 Feb 2024
Publication statusPublished - 7 Mar 2024

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

ASJC Scopus subject areas

Cite this

Structure of the multi-subunit chloroplast RNA polymerase. / do Prado, Paula F V; Ahrens, Frederik M; Liebers, Monique et al.
In: Molecular cell, Vol. 84, No. 5, 07.03.2024, p. 910-925.e5.

Research output: Contribution to journalArticleResearchpeer review

do Prado, PFV, Ahrens, FM, Liebers, M, Ditz, N, Braun, H-P, Pfannschmidt, T & Hillen, H 2024, 'Structure of the multi-subunit chloroplast RNA polymerase', Molecular cell, vol. 84, no. 5, pp. 910-925.e5. https://doi.org/10.1016/j.molcel.2024.02.003
do Prado, P. F. V., Ahrens, F. M., Liebers, M., Ditz, N., Braun, H.-P., Pfannschmidt, T., & Hillen, H. (2024). Structure of the multi-subunit chloroplast RNA polymerase. Molecular cell, 84(5), 910-925.e5. https://doi.org/10.1016/j.molcel.2024.02.003
do Prado PFV, Ahrens FM, Liebers M, Ditz N, Braun HP, Pfannschmidt T et al. Structure of the multi-subunit chloroplast RNA polymerase. Molecular cell. 2024 Mar 7;84(5):910-925.e5. Epub 2024 Feb 29. doi: 10.1016/j.molcel.2024.02.003
do Prado, Paula F V ; Ahrens, Frederik M ; Liebers, Monique et al. / Structure of the multi-subunit chloroplast RNA polymerase. In: Molecular cell. 2024 ; Vol. 84, No. 5. pp. 910-925.e5.
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AU - do Prado, Paula F V

AU - Ahrens, Frederik M

AU - Liebers, Monique

AU - Ditz, Noah

AU - Braun, Hans-Peter

AU - Pfannschmidt, Thomas

AU - Hillen, Hauke

N1 - 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.

PY - 2024/3/7

Y1 - 2024/3/7

N2 - 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.

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KW - cryo-EM

KW - gene expression

KW - organelle

KW - photosynthesis

KW - plastid

KW - RNA

KW - RNA polymerase

KW - structural biology

KW - transcription

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JF - Molecular cell

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