5OLA

Structure of mitochondrial transcription elongation complex in complex with elongation factor TEFM

Summary for 5OLA

• Entry DOI: 10.2210/pdb5ola/pdb
• Descriptor: Transcription elongation factor, mitochondrial, DNA-directed RNA polymerase, mitochondrial, DNA (5'-D(P*AP*TP*GP*GP*TP*GP*TP*AP*AP*CP*GP*CP*CP*AP*GP*AP*CP*GP*AP*AP*C)-3'), ... (5 entities in total)
• Functional Keywords: elongation factor, mitochondria, resolvase, rna polymerase, transcription
• Biological source: Homo sapiens (Human); More
• Cellular location: Mitochondrion matrix : Q96QE5; Mitochondrion: O00411
• Total number of polymer chains: 12
• Total formula weight: 407300.53

Authors

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. (deposition date: 2017-07-27, release date: 2017-10-18, Last modification date: 2024-01-17)

Primary citation

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

Experimental method

X-RAY DIFFRACTION (3.904 Å)