Structural insights into human TFIIIC promoter recognition DOI Creative Commons
Wolfram Seifert-Dávila, Mathias Girbig, Luis Hauptmann

et al.

Science Advances, Journal Year: 2023, Volume and Issue: 9(27)

Published: July 7, 2023

Transcription factor (TF) IIIC recruits RNA polymerase (Pol) III to most of its target genes. Recognition intragenic A- and B-box motifs in transfer (tRNA) genes by TFIIIC modules τA τB is the first critical step for tRNA synthesis but mechanistically poorly understood. Here, we report cryo–electron microscopy structures six-subunit human complex unbound bound a gene. The module recognizes via DNA shape sequence readout through assembly multiple winged-helix domains. TFIIIC220 forms an integral part both connecting two subcomplexes ~550–amino acid residue flexible linker. Our data provide structural mechanism which high-affinity recognition anchors promoter permits scanning low-affinity A-boxes TFIIIB Pol activation.

Language: Английский

The plastid-encoded RNA polymerase of plant chloroplasts DOI Creative Commons
Frederik Ahrens, Paula Favoretti Vital do Prado, Hauke S. Hillen

et al.

Trends in Plant Science, Journal Year: 2025, Volume and Issue: unknown

Published: Feb. 1, 2025

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

Language: Английский

Citations

0
POLR1D, a shared subunit of RNA polymerase I and III, modulates mTORC1 activity DOI
Neuton Gorjão, Lukasz S. Borowski, Roman J. Szczęsny

et al.

Biochimica et Biophysica Acta (BBA) - Molecular Cell Research, Journal Year: 2025, Volume and Issue: unknown, P. 119957 - 119957

Published: April 1, 2025

Language: Английский

Citations

0
PP2A attenuates α-amanitin-induced liver injury by promoting autophagy and inhibiting apoptosis in mouse models DOI
Hui Xu, Jian Sun,

Yu Zhao

et al.

Chemico-Biological Interactions, Journal Year: 2025, Volume and Issue: unknown, P. 111558 - 111558

Published: May 1, 2025

Language: Английский

Citations

0
Regulation of RNA Polymerase I Stability and Function DOI Open Access
Stephanie Pitts, Marikki Laiho

Cancers, Journal Year: 2022, Volume and Issue: 14(23), P. 5776 - 5776

Published: Nov. 24, 2022

RNA polymerase I is a highly processive enzyme with fast initiation and elongation rates. The structure of Pol I, its in-built cleavage ability incorporation subunits homologous to transcription factors, enables it quickly efficiently synthesize the enormous amount rRNA required for ribosome biogenesis. Each step carefully controlled. However, cancers have highjacked these control points switch enzyme, transcription, on permanently. While this provides an exceptional benefit cancer cells, also creates potential therapeutic vulnerability. We review current research regulation we discuss chemical biology efforts develop new targeted agents against process. Lastly, highlight challenges that arisen from introduction promiscuous mechanisms action provide examples specificity selectivity I.

Language: Английский

Citations

15
Structural insights into human TFIIIC promoter recognition DOI Creative Commons
Wolfram Seifert-Dávila, Mathias Girbig, Luis Hauptmann

et al.

Science Advances, Journal Year: 2023, Volume and Issue: 9(27)

Published: July 7, 2023

Transcription factor (TF) IIIC recruits RNA polymerase (Pol) III to most of its target genes. Recognition intragenic A- and B-box motifs in transfer (tRNA) genes by TFIIIC modules τA τB is the first critical step for tRNA synthesis but mechanistically poorly understood. Here, we report cryo–electron microscopy structures six-subunit human complex unbound bound a gene. The module recognizes via DNA shape sequence readout through assembly multiple winged-helix domains. TFIIIC220 forms an integral part both connecting two subcomplexes ~550–amino acid residue flexible linker. Our data provide structural mechanism which high-affinity recognition anchors promoter permits scanning low-affinity A-boxes TFIIIB Pol activation.

Language: Английский

Citations

9