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- EMDB-13735: Mitochondrial DNA dependent RNA polymerase homodimer. -

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Basic information

Entry
Database: EMDB / ID: EMD-13735
TitleMitochondrial DNA dependent RNA polymerase homodimer.
Map data
Sample
  • Complex: POLRMT
    • Complex: Mitochondrial DNA-directed RNA polymerase dimer.
      • Protein or peptide: DNA-directed RNA polymerase, mitochondrialPolymerase
Function / homology
Function and homology information


Mitochondrial transcription initiation / mitochondrial DNA-directed RNA polymerase complex / mitochondrial promoter sequence-specific DNA binding / transcription initiation at mitochondrial promoter / mitochondrial transcription / DNA primase activity / mitochondrial nucleoid / Transcriptional activation of mitochondrial biogenesis / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase ...Mitochondrial transcription initiation / mitochondrial DNA-directed RNA polymerase complex / mitochondrial promoter sequence-specific DNA binding / transcription initiation at mitochondrial promoter / mitochondrial transcription / DNA primase activity / mitochondrial nucleoid / Transcriptional activation of mitochondrial biogenesis / DNA-directed 5'-3' RNA polymerase activity / DNA-directed RNA polymerase / 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. / Tetratricopeptide-like helical domain superfamily / DNA/RNA polymerase superfamily
Similarity search - Domain/homology
DNA-directed RNA polymerase, mitochondrial
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 3.5 Å
AuthorsDas H / Hallberg BM
Funding support1 items
OrganizationGrant numberCountry
Not funded
CitationJournal: Cell / Year: 2022
Title: Non-coding 7S RNA inhibits transcription via mitochondrial RNA polymerase dimerization.
Authors: Xuefeng Zhu / Xie Xie / Hrishikesh Das / Benedict G Tan / Yonghong Shi / Ali Al-Behadili / Bradley Peter / Elisa Motori / Sebastian Valenzuela / Viktor Posse / Claes M Gustafsson / B Martin ...Authors: Xuefeng Zhu / Xie Xie / Hrishikesh Das / Benedict G Tan / Yonghong Shi / Ali Al-Behadili / Bradley Peter / Elisa Motori / Sebastian Valenzuela / Viktor Posse / Claes M Gustafsson / B Martin Hällberg / Maria Falkenberg /
Abstract: The mitochondrial genome encodes 13 components of the oxidative phosphorylation system, and altered mitochondrial transcription drives various human pathologies. A polyadenylated, non-coding RNA ...The mitochondrial genome encodes 13 components of the oxidative phosphorylation system, and altered mitochondrial transcription drives various human pathologies. A polyadenylated, non-coding RNA molecule known as 7S RNA is transcribed from a region immediately downstream of the light strand promoter in mammalian cells, and its levels change rapidly in response to physiological conditions. Here, we report that 7S RNA has a regulatory function, as it controls levels of mitochondrial transcription both in vitro and in cultured human cells. Using cryo-EM, we show that POLRMT dimerization is induced by interactions with 7S RNA. The resulting POLRMT dimer interface sequesters domains necessary for promoter recognition and unwinding, thereby preventing transcription initiation. We propose that the non-coding 7S RNA molecule is a component of a negative feedback loop that regulates mitochondrial transcription in mammalian cells.
History
DepositionOct 13, 2021-
Header (metadata) releaseSep 28, 2022-
Map releaseSep 28, 2022-
UpdateOct 5, 2022-
Current statusOct 5, 2022Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_13735.png

Downloads & links

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Map

FileDownload / File: emd_13735.map.gz / Format: CCP4 / Size: 103 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

Image control

Size
Brightness
Contrast
Others
AxesZ (Sec.)Y (Row.)X (Col.)
1.01 Å/pix.
x 300 pix.
= 303. Å		1.01 Å/pix.
x 300 pix.
= 303. Å		1.01 Å/pix.
x 300 pix.
= 303. Å

Surface

Projections

Slices (1/3)

Slices (1/2)

Slices (2/3)

Images are generated by Spider.

Voxel sizeX=Y=Z: 1.01 Å
Density

Histogram

Histogram (log scale)
Contour LevelBy AUTHOR: 0.27
Minimum - Maximum-1.3951983 - 2.575027
Average (Standard dev.)0.0014780278 (±0.05348014)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions300300300
Spacing300300300
CellA=B=C: 303.0 Å
α=β=γ: 90.0 °

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Supplemental data

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Additional map: localized reconstruction

Fileemd_13735_additional_1.map
Annotationlocalized reconstruction
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Additional map: localized reconstruction

Fileemd_13735_additional_2.map
Annotationlocalized reconstruction
Projections & Slices
AxesZYX

Projections

Slices (1/2)
Density Histograms

Histogram

Histogram (log scale)

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Sample components

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Entire : POLRMT

EntireName: POLRMT
Components
  • Complex: POLRMT
    • Complex: Mitochondrial DNA-directed RNA polymerase dimer.
      • Protein or peptide: DNA-directed RNA polymerase, mitochondrialPolymerase

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Supramolecule #1: POLRMT

SupramoleculeName: POLRMT / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all / Details: DNA-directed RNA polymerase, mitochondrial
Molecular weightTheoretical: 137 KDa

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Supramolecule #2: Mitochondrial DNA-directed RNA polymerase dimer.

SupramoleculeName: Mitochondrial DNA-directed RNA polymerase dimer. / type: complex / Chimera: Yes / ID: 2 / Parent: 1 / Macromolecule list: all / Details: DNA-directed RNA polymerase dimer, mitochondrial
Source (natural)Organism: Homo sapiens (human)
Recombinant expressionOrganism: Escherichia coli (E. coli)

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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: 2 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 137.292125 KDa
Recombinant expressionOrganism: Escherichia coli (E. coli)
SequenceString: MHHHHHHTSG VDLGTENLYF QSSSASPQEQ DQDRRKDWGH VELLEVLQAR VRQLQAESVS EVVVNRVDVA RLPECGSGDG SLQPPRKVQ MGAKDATPVP CGRWAKILEK DKRTQQMRMQ RLKAKLQMPF QSGEFKALTR RLQVEPRLLS KQMAGCLEDC T RQAPESPW ...String:
MHHHHHHTSG VDLGTENLYF QSSSASPQEQ DQDRRKDWGH VELLEVLQAR VRQLQAESVS EVVVNRVDVA RLPECGSGDG SLQPPRKVQ MGAKDATPVP CGRWAKILEK DKRTQQMRMQ RLKAKLQMPF QSGEFKALTR RLQVEPRLLS KQMAGCLEDC T RQAPESPW EEQLARLLQE APGKLSLDVE QAPSGQHSQA QLSGQQQRLL AFFKCCLLTD QLPLAHHLLV VHHGQRQKRK LL TLDMYNA VMLGWARQGA FKELVYVLFM VKDAGLTPDL LSYAAALQCM GRQDQDAGTI ERCLEQMSQE GLKLQALFTA VLL SEEDRA TVLKAVHKVK PTFSLPPQLP PPVNTSKLLR DVYAKDGRVS YPKLHLPLKT LQCLFEKQLH MELASRVCVV SVEK PTLPS KEVKHARKTL KTLRDQWEKA LCRALRETKN RLEREVYEGR FSLYPFLCLL DEREVVRMLL QVLQALPAQG ESFTT LARE LSARTFSRHV VQRQRVSGQV QALQNHYRKY LCLLASDAEV PEPCLPRQYW EELGAPEALR EQPWPLPVQM ELGKLL AEM LVQATQMPCS LDKPHRSSRL VPVLYHVYSF RNVQQIGILK PHPAYVQLLE KAAEPTLTFE AVDVPMLCPP LPWTSPH SG AFLLSPTKLM RTVEGATQHQ ELLETCPPTA LHGALDALTQ LGNCAWRVNG RVLDLVLQLF QAKGCPQLGV PAPPSEAP Q PPEAHLPHSA APARKAELRR ELAHCQKVAR EMHSLRAEAL YRLSLAQHLR DRVFWLPHNM DFRGRTYPCP PHFNHLGSD VARALLEFAQ GRPLGPHGLD WLKIHLVNLT GLKKREPLRK RLAFAEEVMD DILDSADQPL TGRKWWMGAE EPWQTLACCM EVANAVRAS DPAAYVSHLP VHQDGSCNGL QHYAALGRDS VGAASVNLEP SDVPQDVYSG VAAQVEVFRR QDAQRGMRVA Q VLEGFITR KVVKQTVMTV VYGVTRYGGR LQIEKRLREL SDFPQEFVWE ASHYLVRQVF KSLQEMFSGT RAIQHWLTES AR LISHMGS VVEWVTPLGV PVIQPYRLDS KVKQIGGGIQ SITYTHNGDI SRKPNTRKQK NGFPPNFIHS LDSSHMMLTA LHC YRKGLT FVSVHDCYWT HAADVSVMNQ VCREQFVRLH SEPILQDLSR FLVKRFCSEP QKILEASQLK ETLQAVPKPG AFDL EQVKR STYFFS

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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

Concentration2.1 mg/mL
BufferpH: 8
VitrificationCryogen name: ETHANE / Chamber humidity: 100 % / Chamber temperature: 277 K / Instrument: FEI VITROBOT MARK IV

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Electron microscopy

MicroscopeTFS KRIOS
Electron beamAcceleration voltage: 300 kV / Electron source: FIELD EMISSION GUN
Electron opticsC2 aperture diameter: 20.0 µm / Calibrated defocus min: 0.3 µm / Illumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELDBright-field microscopy / Cs: 2.7 mm / Nominal defocus max: 2.5 µm / Nominal defocus min: 0.3 µm / Nominal magnification: 165000
Specialist opticsEnergy filter - Name: GIF Bioquantum / Energy filter - Slit width: 10 eV
Sample stageSpecimen holder model: FEI TITAN KRIOS AUTOGRID HOLDER / Cooling holder cryogen: NITROGEN
Image recordingFilm or detector model: GATAN K3 BIOQUANTUM (6k x 4k) / Number grids imaged: 5 / Number real images: 42131 / Average exposure time: 1.5 sec. / Average electron dose: 48.6 e/Å2
Experimental equipment
Model: Titan Krios / Image courtesy: FEI Company

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Image processing

CTF correctionSoftware - Name: cryoSPARC (ver. 3.2.0)
Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

3spa

Initial angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 3.2.0)
Final 3D classificationSoftware: (Name: cryoSPARC (ver. 3.2.0), RELION (ver. 3.1))
Final angle assignmentType: PROJECTION MATCHING / Software - Name: cryoSPARC (ver. 3.2.0)
Final reconstructionApplied symmetry - Point group: C1 (asymmetric) / Resolution.type: BY AUTHOR / Resolution: 3.5 Å / Resolution method: FSC 0.143 CUT-OFF / Software - Name: cryoSPARC (ver. 3.2.0) / Number images used: 13500

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Atomic model buiding 1

Initial modelPDB ID:

3spa

RefinementSpace: REAL / Protocol: OTHER
Output model

PDB-7pzp:
Mitochondrial DNA dependent RNA polymerase homodimer.

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