5OL8

Structure of human mitochondrial transcription elongation factor (TEFM) C-terminal domain

5OL8 の概要

• エントリーDOI: 10.2210/pdb5ol8/pdb
• 分子名称: Transcription elongation factor, mitochondrial, GLYCEROL (3 entities in total)
• 機能のキーワード: elongation factor, mitochondria, resolvase, rna polymerase, transcription
• 由来する生物種: Homo sapiens (Human)
• 細胞内の位置: Mitochondrion matrix : Q96QE5
• タンパク質・核酸の鎖数: 4
• 化学式量合計: 149119.52

構造登録者

Hillen, H.S.,Parshin, A.V.,Agaronyan, K.,Morozov, Y.,Graber, J.J.,Chernev, A.,Schwinghammer, K.,Urlaub, H.,Anikin, M.,Cramer, P.,Temiakov, D. (登録日: 2017-07-27, 公開日: 2017-10-18, 最終更新日: 2024-05-08)

主引用文献

Hillen, H.S.,Parshin, A.V.,Agaronyan, K.,Morozov, Y.I.,Graber, J.J.,Chernev, A.,Schwinghammer, K.,Urlaub, H.,Anikin, M.,Cramer, P.,Temiakov, D.
Mechanism of Transcription Anti-termination in Human Mitochondria.
Cell, 171:1082-1093.e13, 2017

PubMed Abstract: In human mitochondria, transcription termination events at a G-quadruplex region near the replication origin are thought to drive replication of mtDNA by generation of an RNA primer. This process is suppressed by a key regulator of mtDNA-the transcription factor TEFM. We determined the structure of an anti-termination complex in which TEFM is bound to transcribing mtRNAP. The structure reveals interactions of the dimeric pseudonuclease core of TEFM with mobile structural elements in mtRNAP and the nucleic acid components of the elongation complex (EC). Binding of TEFM to the DNA forms a downstream "sliding clamp," providing high processivity to the EC. TEFM also binds near the RNA exit channel to prevent formation of the RNA G-quadruplex structure required for termination and thus synthesis of the replication primer. Our data provide insights into target specificity of TEFM and mechanisms by which it regulates the switch between transcription and replication of mtDNA.

PubMed: 29033127
DOI: 10.1016/j.cell.2017.09.035

実験手法

X-RAY DIFFRACTION (1.9 Å)