The plastid-encoded RNA polymerase of plant chloroplasts

verfasst von: Frederik M. Ahrens, Paula F.V. do Prado, Hauke S. Hillen, Thomas Pfannschmidt
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.
Organisationseinheit(en): Institut für Botanik
Externe Organisation(en): Georg-August-Universität Göttingen
Max-Planck-Institut für Multidisziplinäre Naturwissenschaften
Typ: Übersichtsarbeit
Journal: Trends in plant science
ISSN: 1360-1385
Publikationsdatum: 25.02.2025
Publikationsstatus: Elektronisch veröffentlicht (E-Pub)
Peer-reviewed: Ja
ASJC Scopus Sachgebiete: Pflanzenkunde
Elektronische Version(en): https://doi.org/10.1016/j.tplants.2025.01.010 (Zugang: Offen)

BibTeX

@article{e615ca6c1ac54c2786ea2bebab7682e0,
title = "The plastid-encoded RNA polymerase of plant chloroplasts",
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.",
keywords = "chloroplast, cryo-EM structures, functional predictions, PEP-associated proteins, RNA polymerase, transcription",
author = "Ahrens, {Frederik M.} and {do Prado}, {Paula F.V.} and Hillen, {Hauke S.} and Thomas Pfannschmidt",
note = "Publisher Copyright: {\textcopyright} 2025 The Author(s)",
year = "2025",
month = feb,
day = "25",
doi = "10.1016/j.tplants.2025.01.010",
language = "English",
journal = "Trends in plant science",
issn = "1360-1385",
publisher = "Elsevier Ltd.",
}