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-Structure paper
Title | Cryo-EM structures of the plant plastid-encoded RNA polymerase. |
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Journal, issue, pages | Cell, Vol. 187, Issue 5, Page 1127-1144.e21, Year 2024 |
Publish date | Feb 29, 2024 |
Authors | Xiao-Xian Wu / Wen-Hui Mu / Fan Li / Shu-Yi Sun / Chao-Jun Cui / Chanhong Kim / Fei Zhou / Yu Zhang / |
PubMed Abstract | Chloroplasts are green plastids in the cytoplasm of eukaryotic algae and plants responsible for photosynthesis. The plastid-encoded RNA polymerase (PEP) plays an essential role during chloroplast ...Chloroplasts are green plastids in the cytoplasm of eukaryotic algae and plants responsible for photosynthesis. The plastid-encoded RNA polymerase (PEP) plays an essential role during chloroplast biogenesis from proplastids and functions as the predominant RNA polymerase in mature chloroplasts. The PEP-centered transcription apparatus comprises a bacterial-origin PEP core and more than a dozen eukaryotic-origin PEP-associated proteins (PAPs) encoded in the nucleus. Here, we determined the cryo-EM structures of Nicotiana tabacum (tobacco) PEP-PAP apoenzyme and PEP-PAP transcription elongation complexes at near-atomic resolutions. Our data show the PEP core adopts a typical fold as bacterial RNAP. Fifteen PAPs bind at the periphery of the PEP core, facilitate assembling the PEP-PAP supercomplex, protect the complex from oxidation damage, and likely couple gene transcription with RNA processing. Our results report the high-resolution architecture of the chloroplast transcription apparatus and provide the structural basis for the mechanistic and functional study of transcription regulation in chloroplasts. |
External links | Cell / PubMed:38428393 |
Methods | EM (single particle) |
Resolution | 2.7 - 3.0 Å |
Structure data | EMDB-37386, PDB-8w9z: EMDB-37387, PDB-8wa0: EMDB-37388, PDB-8wa1: |
Chemicals | ChemComp-ZN: ChemComp-MG: ChemComp-FE: |
Source |
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Keywords | TRANSCRIPTION / PEP / PAP |