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The plastid-encoded RNA polymerase of plant chloroplasts

Publikation: Beitrag in FachzeitschriftÜbersichtsarbeitForschungPeer-Review

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Externe Organisationen

  • Georg-August-Universität Göttingen
  • Max-Planck-Institut für Multidisziplinäre Naturwissenschaften

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OriginalspracheEnglisch
FachzeitschriftTrends in plant science
PublikationsstatusElektronisch veröffentlicht (E-Pub) - 25 Feb. 2025

Abstract

Plant chloroplasts possess a dedicated genome (plastome) and a prokaryotic-type plastid-encoded RNA polymerase (PEP) that mediates its expression. PEP is composed of five bacteria-like core proteins and 16 nucleus-encoded PEP-associated proteins (PAPs). These are essential for PEP-driven transcription and chloroplast biogenesis, but their functions and structural arrangement in the PEP complex remained largely enigmatic. Recently, four independently determined cryogenic-electron microscopy (cryo-EM) structures of purified plant PEP complexes reported features of the prokaryotic core and the arrangement of PAPs around it, identified potential functional domains and cofactors, and described the interactions of PEP with DNA. We explore these data and critically discuss the proposed regulatory impact of PAPs on the transcription process. We further address the evolutionary implications and describe fields for future investigation.

ASJC Scopus Sachgebiete

Zitieren

The plastid-encoded RNA polymerase of plant chloroplasts. / Ahrens, Frederik M.; do Prado, Paula F.V.; Hillen, Hauke S. et al.
in: Trends in plant science, 25.02.2025.

Publikation: Beitrag in FachzeitschriftÜbersichtsarbeitForschungPeer-Review

Ahrens FM, do Prado PFV, Hillen HS, Pfannschmidt T. The plastid-encoded RNA polymerase of plant chloroplasts. Trends in plant science. 2025 Feb 25. Epub 2025 Feb 25. doi: 10.1016/j.tplants.2025.01.010
Ahrens, Frederik M. ; do Prado, Paula F.V. ; Hillen, Hauke S. et al. / The plastid-encoded RNA polymerase of plant chloroplasts. in: Trends in plant science. 2025.
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AU - Ahrens, Frederik M.

AU - do Prado, Paula F.V.

AU - Hillen, Hauke S.

AU - Pfannschmidt, Thomas

N1 - Publisher Copyright: © 2025 The Author(s)

PY - 2025/2/25

Y1 - 2025/2/25

N2 - Plant chloroplasts possess a dedicated genome (plastome) and a prokaryotic-type plastid-encoded RNA polymerase (PEP) that mediates its expression. PEP is composed of five bacteria-like core proteins and 16 nucleus-encoded PEP-associated proteins (PAPs). These are essential for PEP-driven transcription and chloroplast biogenesis, but their functions and structural arrangement in the PEP complex remained largely enigmatic. Recently, four independently determined cryogenic-electron microscopy (cryo-EM) structures of purified plant PEP complexes reported features of the prokaryotic core and the arrangement of PAPs around it, identified potential functional domains and cofactors, and described the interactions of PEP with DNA. We explore these data and critically discuss the proposed regulatory impact of PAPs on the transcription process. We further address the evolutionary implications and describe fields for future investigation.

AB - Plant chloroplasts possess a dedicated genome (plastome) and a prokaryotic-type plastid-encoded RNA polymerase (PEP) that mediates its expression. PEP is composed of five bacteria-like core proteins and 16 nucleus-encoded PEP-associated proteins (PAPs). These are essential for PEP-driven transcription and chloroplast biogenesis, but their functions and structural arrangement in the PEP complex remained largely enigmatic. Recently, four independently determined cryogenic-electron microscopy (cryo-EM) structures of purified plant PEP complexes reported features of the prokaryotic core and the arrangement of PAPs around it, identified potential functional domains and cofactors, and described the interactions of PEP with DNA. We explore these data and critically discuss the proposed regulatory impact of PAPs on the transcription process. We further address the evolutionary implications and describe fields for future investigation.

KW - chloroplast

KW - cryo-EM structures

KW - functional predictions

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KW - RNA polymerase

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