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- EMDB-51729: Cryo-EM structure of the human mitochondrial RNA polymerase trans... -

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Entry
Database: EMDB / ID: EMD-51729
TitleCryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)
Map data
Sample
  • Complex: Cryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)
    • Organelle or cellular component: DNA-directed RNA polymerase, mitochondrial
      • Protein or peptide: DNA-directed RNA polymerase, mitochondrial
    • Organelle or cellular component: DNA (56-mer)
      • DNA: Non-template strand DNA (56-MER)
      • DNA: Template strand DNA (56-MER)
    • Organelle or cellular component: Dimethyladenosine transferase 2, mitochondrial
      • Protein or peptide: Dimethyladenosine transferase 2, mitochondrial
    • RNA: RNA (5'-D(*(GTP))-R(P*GP*A)-3')
KeywordsPOLRMT / TFB2M / TFAM / transcription initiation / polymerase / h-mtRNAP / mtRNAP / RNA polymerase / mitochondrial DNA / mitochondria / slippage / TRANSCRIPTION
Function / homology
Function and homology information


rRNA (adenine-N6-)-methyltransferase activity / Mitochondrial transcription initiation / mitochondrial DNA-directed RNA polymerase complex / mitochondrial transcription factor activity / mitochondrial promoter sequence-specific DNA binding / transcription initiation at mitochondrial promoter / rRNA (adenine-N6,N6-)-dimethyltransferase activity / Strand-asynchronous mitochondrial DNA replication / mitochondrial DNA replication / mitochondrial transcription ...rRNA (adenine-N6-)-methyltransferase activity / Mitochondrial transcription initiation / mitochondrial DNA-directed RNA polymerase complex / mitochondrial transcription factor activity / mitochondrial promoter sequence-specific DNA binding / transcription initiation at mitochondrial promoter / rRNA (adenine-N6,N6-)-dimethyltransferase activity / Strand-asynchronous mitochondrial DNA replication / mitochondrial DNA replication / mitochondrial transcription / rRNA methylation / mitochondrial nucleoid / Transferases; Transferring one-carbon groups; Methyltransferases / Transcriptional activation of mitochondrial biogenesis / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / 3'-5'-RNA exonuclease activity / sequence-specific DNA binding / mitochondrial matrix / protein-containing complex / mitochondrion / RNA binding
Similarity search - Function
DNA-directed RNA polymerase, N-terminal / DNA-directed RNA polymerase, N-terminal domain superfamily / DNA-directed RNA polymerase N-terminal / Bacteriophage-type RNA polymerase family active site signature 1. / DNA-directed RNA polymerase N-terminal / DNA-directed RNA polymerase, phage-type / : / DNA-dependent RNA polymerase / Bacteriophage-type RNA polymerase family active site signature 2. / Ribosomal RNA adenine methylase transferase, N-terminal ...DNA-directed RNA polymerase, N-terminal / DNA-directed RNA polymerase, N-terminal domain superfamily / DNA-directed RNA polymerase N-terminal / Bacteriophage-type RNA polymerase family active site signature 1. / DNA-directed RNA polymerase N-terminal / DNA-directed RNA polymerase, phage-type / : / DNA-dependent RNA polymerase / Bacteriophage-type RNA polymerase family active site signature 2. / Ribosomal RNA adenine methylase transferase, N-terminal / Ribosomal RNA adenine dimethylases / Ribosomal RNA adenine methyltransferase KsgA/Erm / Ribosomal RNA adenine dimethylase / rRNA adenine N(6)-methyltransferase family profile. / Tetratricopeptide-like helical domain superfamily / S-adenosyl-L-methionine-dependent methyltransferase superfamily / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
DNA-directed RNA polymerase, mitochondrial / Dimethyladenosine transferase 2, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human) / synthetic construct (others)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.15 Å
AuthorsGoovaerts Q / Shen J / Ajjugal Y / De Wijngaert B / Patel SS / Das K
Funding support Belgium, 1 items
OrganizationGrant numberCountry
Research Foundation - Flanders (FWO)1162823N Belgium
CitationJournal: Mol Cell / Year: 2025
Title: Human mitochondrial RNA polymerase structures reveal transcription start site and slippage mechanism.
Authors: Jiayu Shen / Quinten Goovaerts / Yogeeshwar Ajjugal / Brent De Wijngaert / Kalyan Das / Smita S Patel /
Abstract: Transcription of the human mitochondrial DNA is initiated by POLRMT and initiation factors mitochondrial transcription factor A (TFAM) and mitochondrial transcription factor B2 (TFB2M). We present ...Transcription of the human mitochondrial DNA is initiated by POLRMT and initiation factors mitochondrial transcription factor A (TFAM) and mitochondrial transcription factor B2 (TFB2M). We present cryo-electron microscopy (cryo-EM) structures of three transcription initiation intermediates (pre-catalytic IC3 [pre-IC3], slipped-IC3, and slipped pre-IC4) catalyzing RNA synthesis by normal and slippage pathways with fully resolved transcription bubbles and RNA transcripts starting from the +1 or -1 position. The structural and biochemical studies reveal mechanisms of promoter melting, start site selection, and slippage synthesis. Promoter melting begins at -4 with base-specific interactions of template -4 and -3 guanines with POLRMT and non-template -1 adenine with TFB2M. The NT-stabilizing loop (KLDPRSGGVIKPP) and Y209 of TFB2M and W1026 of POLRMT interact with the non-template strand to guide initiation from the +1 start site. The -1 position is not an alternative start site but supports slippage initiation by base-pairing with a slipped or rebound 2-nt RNA. Cryo-EM resolved additional apo and dimeric complexes whose populations may regulate transcription initiation.
History
DepositionOct 4, 2024-
Header (metadata) releaseJul 30, 2025-
Map releaseJul 30, 2025-
UpdateAug 6, 2025-
Current statusAug 6, 2025Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_51729.png

Downloads & links

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Map

FileDownload / File: emd_51729.map.gz / Format: CCP4 / Size: 10.5 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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AxesZ (Sec.)Y (Row.)X (Col.)
0.97 Å/pix.
x 140 pix.
= 135.8 Å		0.97 Å/pix.
x 140 pix.
= 135.8 Å		0.97 Å/pix.
x 140 pix.
= 135.8 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 0.97 Å
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Histogram (log scale)
Contour LevelBy AUTHOR: 0.00659
Minimum - Maximum-0.03721126 - 0.08552017
Average (Standard dev.)0.0008986678 (±0.0065938216)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions140140140
Spacing140140140
CellA=B=C: 135.8 Å
α=β=γ: 90.0 °

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Supplemental data

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Mask #1

Fileemd_51729_msk_1.map
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Additional map: #1

Fileemd_51729_additional_1.map
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Half map: #2

Fileemd_51729_half_map_1.map
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Half map: #1

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Sample components

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Entire : Cryo-EM structure of the human mitochondrial RNA polymerase trans...

EntireName: Cryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)
Components
  • Complex: Cryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)
    • Organelle or cellular component: DNA-directed RNA polymerase, mitochondrial
      • Protein or peptide: DNA-directed RNA polymerase, mitochondrial
    • Organelle or cellular component: DNA (56-mer)
      • DNA: Non-template strand DNA (56-MER)
      • DNA: Template strand DNA (56-MER)
    • Organelle or cellular component: Dimethyladenosine transferase 2, mitochondrial
      • Protein or peptide: Dimethyladenosine transferase 2, mitochondrial
    • RNA: RNA (5'-D(*(GTP))-R(P*GP*A)-3')

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Supramolecule #1: Cryo-EM structure of the human mitochondrial RNA polymerase trans...

SupramoleculeName: Cryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)
type: complex / ID: 1 / Parent: 0 / Macromolecule list: #1-#5
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 240 KDa

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Supramolecule #2: DNA-directed RNA polymerase, mitochondrial

SupramoleculeName: DNA-directed RNA polymerase, mitochondrial / type: organelle_or_cellular_component / ID: 2 / Parent: 1 / Macromolecule list: #1
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #3: DNA (56-mer)

SupramoleculeName: DNA (56-mer) / type: organelle_or_cellular_component / ID: 3 / Parent: 1 / Macromolecule list: #2-#3
Source (natural)Organism: Homo sapiens (human)

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Supramolecule #4: Dimethyladenosine transferase 2, mitochondrial

SupramoleculeName: Dimethyladenosine transferase 2, mitochondrial / type: organelle_or_cellular_component / ID: 4 / Parent: 1 / Macromolecule list: #4
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: DNA-directed RNA polymerase, mitochondrial

MacromoleculeName: DNA-directed RNA polymerase, mitochondrial / type: protein_or_peptide / ID: 1 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 134.632344 KDa
Recombinant expressionOrganism: Escherichia coli BL21 (bacteria)
SequenceString: SASPQEQDQD RRKDWGHVEL LEVLQARVRQ LQAESVSEVV VNRVDVARLP ECGSGDGSLQ PPRKVQMGAK DATPVPCGRW AKILEKDKR TQQMRMQRLK AKLQMPFQSG EFKALTRRLQ VEPRLLSKQM AGCLEDCTRQ APESPWEEQL ARLLQEAPGK L SLDVEQAP ...String:
SASPQEQDQD RRKDWGHVEL LEVLQARVRQ LQAESVSEVV VNRVDVARLP ECGSGDGSLQ PPRKVQMGAK DATPVPCGRW AKILEKDKR TQQMRMQRLK AKLQMPFQSG EFKALTRRLQ VEPRLLSKQM AGCLEDCTRQ APESPWEEQL ARLLQEAPGK L SLDVEQAP SGQHSQAQLS GQQQRLLAFF KCCLLTDQLP LAHHLLVVHH GQRQKRKLLT LDMYNAVMLG WARQGAFKEL VY VLFMVKD AGLTPDLLSY AAALQCMGRQ DQDAGTIERC LEQMSQEGLK LQALFTAVLL SEEDRATVLK AVHKVKPTFS LPP QLPPPV NTSKLLRDVY AKDGRVSYPK LHLPLKTLQC LFEKQLHMEL ASRVCVVSVE KPTLPSKEVK HARKTLKTLR DQWE KALCR ALRETKNRLE REVYEGRFSL YPFLCLLDER EVVRMLLQVL QALPAQGESF TTLARELSAR TFSRHVVQRQ RVSGQ VQAL QNHYRKYLCL LASDAEVPEP CLPRQYWEEL GAPEALREQP WPLPVQMELG KLLAEMLVQA TQMPCSLDKP HRSSRL VPV LYHVYSFRNV QQIGILKPHP AYVQLLEKAA EPTLTFEAVD VPMLCPPLPW TSPHSGAFLL SPTKLMRTVE GATQHQE LL ETCPPTALHG ALDALTQLGN CAWRVNGRVL DLVLQLFQAK GCPQLGVPAP PSEAPQPPEA HLPHSAAPAR KAELRREL A HCQKVAREMH SLRAEALYRL SLAQHLRDRV FWLPHNMDFR GRTYPCPPHF NHLGSDVARA LLEFAQGRPL GPHGLDWLK IHLVNLTGLK KREPLRKRLA FAEEVMDDIL DSADQPLTGR KWWMGAEEPW QTLACCMEVA NAVRASDPAA YVSHLPVHQD GSCNGLQHY AALGRDSVGA ASVNLEPSDV PQDVYSGVAA QVEVFRRQDA QRGMRVAQVL EGFITRKVVK QTVMTVVYGV T RYGGRLQI EKRLRELSDF PQEFVWEASH YLVRQVFKSL QEMFSGTRAI QHWLTESARL ISHMGSVVEW VTPLGVPVIQ PY RLDSKVK QIGGGIQSIT YTHNGDISRK PNTRKQKNGF PPNFIHSLDS SHMMLTALHC YRKGLTFVSV HDCYWTHAAD VSV MNQVCR EQFVRLHSEP ILQDLSRFLV KRFCSEPQKI LEASQLKETL QAVPKPGAFD LEQVKRSTYF FS

UniProtKB: DNA-directed RNA polymerase, mitochondrial

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Macromolecule #4: Dimethyladenosine transferase 2, mitochondrial

MacromoleculeName: Dimethyladenosine transferase 2, mitochondrial / type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
EC number: Transferases; Transferring one-carbon groups; Methyltransferases
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 38.901309 KDa
Recombinant expressionOrganism: Escherichia coli B (bacteria)
SequenceString: PPRKASKASL DFKRYVTDRR LAETLAQIYL GKPSRPPHLL LECNPGPGIL TQALLEAGAK VVALESDKTF IPHLESLGKN LDGKLRVIH CDFFKLDPRS GGVIKPPAMS SRGLFKNLGI EAVPWTADIP LKVVGMFPSR GEKRALWKLA YDLYSCTSIY K FGRIEVNM ...String:
PPRKASKASL DFKRYVTDRR LAETLAQIYL GKPSRPPHLL LECNPGPGIL TQALLEAGAK VVALESDKTF IPHLESLGKN LDGKLRVIH CDFFKLDPRS GGVIKPPAMS SRGLFKNLGI EAVPWTADIP LKVVGMFPSR GEKRALWKLA YDLYSCTSIY K FGRIEVNM FIGEKEFQKL MADPGNPDLY HVLSVIWQLA CEIKVLHMEP WSSFDIYTRK GPLENPKRRE LLDQLQQKLY LI QMIPRQN LFTKNLTPMN YNIFFHLLKH CFGRRSATVI DHLRSLTPLD ARDILMQIGK QEDEKVVNMH PQDFKTLFET IER SKDCAY KWLYDETLED R

UniProtKB: Dimethyladenosine transferase 2, mitochondrial

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Macromolecule #2: Non-template strand DNA (56-MER)

MacromoleculeName: Non-template strand DNA (56-MER) / type: dna / ID: 2 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 19.652648 KDa
SequenceString: (DA)(DT)(DG)(DT)(DG)(DT)(DT)(DA)(DG)(DT) (DT)(DG)(DG)(DG)(DG)(DG)(DG)(DT)(DG)(DA) (DC)(DT)(DG)(DT)(DT)(DA)(DA)(DA)(DA) (DG)(DT)(DG)(DC)(DA)(DT)(DA)(DC)(DC)(DG) (DA) (DA)(DC)(DA)(DA)(DA)(DG) ...String:
(DA)(DT)(DG)(DT)(DG)(DT)(DT)(DA)(DG)(DT) (DT)(DG)(DG)(DG)(DG)(DG)(DG)(DT)(DG)(DA) (DC)(DT)(DG)(DT)(DT)(DA)(DA)(DA)(DA) (DG)(DT)(DG)(DC)(DA)(DT)(DA)(DC)(DC)(DG) (DA) (DA)(DC)(DA)(DA)(DA)(DG)(DA)(DT) (DA)(DA)(DA)(DA)(DT)(DT)(DT)(DG)(DA)(DA) (DA)(DT) (DC)(DT)(DG)

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Macromolecule #3: Template strand DNA (56-MER)

MacromoleculeName: Template strand DNA (56-MER) / type: dna / ID: 3 / Number of copies: 1 / Classification: DNA
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 18.867131 KDa
SequenceString: (DC)(DA)(DG)(DT)(DT)(DT)(DC)(DA)(DA)(DA) (DT)(DT)(DT)(DT)(DA)(DT)(DC)(DT)(DC)(DC) (DA)(DG)(DG)(DC)(DG)(DG)(DT)(DA)(DT) (DG)(DC)(DA)(DC)(DT)(DT)(DT)(DT)(DA)(DA) (DC) (DA)(DG)(DT)(DC)(DA)(DC) ...String:
(DC)(DA)(DG)(DT)(DT)(DT)(DC)(DA)(DA)(DA) (DT)(DT)(DT)(DT)(DA)(DT)(DC)(DT)(DC)(DC) (DA)(DG)(DG)(DC)(DG)(DG)(DT)(DA)(DT) (DG)(DC)(DA)(DC)(DT)(DT)(DT)(DT)(DA)(DA) (DC) (DA)(DG)(DT)(DC)(DA)(DC)(DC)(DC) (DC)(DC)(DC)(DA)(DA)(DC)(DT)(DA)(DA)(DC) (DA)(DC) (DA)(DT)

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Macromolecule #5: RNA (5'-D(*(GTP))-R(P*GP*A)-3')

MacromoleculeName: RNA (5'-D(*(GTP))-R(P*GP*A)-3') / type: rna / ID: 5 / Number of copies: 1
Source (natural)Organism: synthetic construct (others)
Molecular weightTheoretical: 1.134619 KDa
SequenceString:
(GTP)GA

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Experimental details

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Structure determination

Methodcryo EM
Processingsingle particle reconstruction
Aggregation stateparticle

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Sample preparation

Concentration0.3 mg/mL
BufferpH: 8
Details: 30 mM Tris-HCl pH 8, 200 mM NaCl, 3 mM DTT, 10 mM MgCl2, 0.01% BOG
GridModel: Quantifoil R1.2/1.3 / Material: GOLD / Mesh: 300 / Support film - Material: CARBON / Support film - topology: HOLEY / Pretreatment - Type: GLOW DISCHARGE / Pretreatment - Time: 45 sec. / Pretreatment - Atmosphere: AIR / Pretreatment - Pressure: 0.03 kPa
VitrificationCryogen name: ETHANE / Chamber humidity: 95 % / Chamber temperature: 281.15 K / Instrument: LEICA PLUNGER
Details: incubated on the grid for 10 seconds prior to back-blotting for 12 seconds.

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Electron microscopy

MicroscopeTFS GLACIOS
Image recordingFilm or detector model: FEI FALCON III (4k x 4k) / Detector mode: COUNTING / Number grids imaged: 1 / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 50.0 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Cs: 2.7 mm / Nominal defocus max: 1.8 µm / Nominal defocus min: 0.6 µm / Nominal magnification: 150000
Sample stageSpecimen holder model: OTHER / Cooling holder cryogen: NITROGEN

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Image processing

CTF correctionType: NONE
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

6erp

Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.15 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: Coot / Number images used: 277033
Initial angle assignmentType: MAXIMUM LIKELIHOOD
Final angle assignmentType: MAXIMUM LIKELIHOOD

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Atomic model buiding 1

RefinementProtocol: FLEXIBLE FIT / Overall B value: 72
Output model

PDB-9gzo:
Cryo-EM structure of the human mitochondrial RNA polymerase transcription initiation complex (POLRMT/TFB2M/DNA/RNA) without TFAM; and with a slipped 3-mer RNA, pppGpGpA (slipped IC3-TFAM)

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