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- EMDB-15135: Human RNA polymerase I -

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Basic information

Entry
Database: EMDB / ID: EMD-15135
TitleHuman RNA polymerase I
Map data
Sample
  • Complex: RNA polymerase I
    • Protein or peptide: x 12 types
KeywordsRNA polymerase I / human rDNA transcription / TRANSCRIPTION
Function / homology
Function and homology information


RNA polymerase I transcription regulator complex / negative regulation of protein localization to nucleolus / nucleologenesis / neural crest formation / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / RNA polymerase I general transcription initiation factor binding / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like complex ...RNA polymerase I transcription regulator complex / negative regulation of protein localization to nucleolus / nucleologenesis / neural crest formation / RNA Polymerase III Chain Elongation / RNA Polymerase III Transcription Termination / DNA/RNA hybrid binding / RNA polymerase I general transcription initiation factor binding / regulation of transcription by RNA polymerase I / RPAP3/R2TP/prefoldin-like complex / RNA Polymerase III Transcription Initiation From Type 1 Promoter / RNA Polymerase III Transcription Initiation From Type 2 Promoter / RNA Polymerase III Transcription Initiation From Type 3 Promoter / Cytosolic sensors of pathogen-associated DNA / RNA polymerase I preinitiation complex assembly / RNA Polymerase III Abortive And Retractive Initiation / nucleobase-containing compound metabolic process / Abortive elongation of HIV-1 transcript in the absence of Tat / RNA Polymerase I Transcription Termination / FGFR2 alternative splicing / MicroRNA (miRNA) biogenesis / Viral Messenger RNA Synthesis / Signaling by FGFR2 IIIa TM / RNA Pol II CTD phosphorylation and interaction with CE during HIV infection / RNA Pol II CTD phosphorylation and interaction with CE / Formation of the Early Elongation Complex / Formation of the HIV-1 Early Elongation Complex / HIV Transcription Initiation / RNA Polymerase II HIV Promoter Escape / Transcription of the HIV genome / RNA Polymerase II Promoter Escape / RNA Polymerase II Transcription Pre-Initiation And Promoter Opening / RNA Polymerase II Transcription Initiation / RNA Polymerase II Transcription Initiation And Promoter Clearance / mRNA Capping / termination of RNA polymerase I transcription / nucleolar large rRNA transcription by RNA polymerase I / mRNA Splicing - Minor Pathway / transcription initiation at RNA polymerase I promoter / PIWI-interacting RNA (piRNA) biogenesis / RNA Polymerase I Transcription Initiation / rRNA transcription / Processing of Capped Intron-Containing Pre-mRNA / Pausing and recovery of Tat-mediated HIV elongation / Tat-mediated HIV elongation arrest and recovery / RNA polymerase II transcribes snRNA genes / HIV elongation arrest and recovery / Pausing and recovery of HIV elongation / transcription by RNA polymerase III / Tat-mediated elongation of the HIV-1 transcript / Formation of HIV-1 elongation complex containing HIV-1 Tat / RNA polymerase I complex / transcription elongation by RNA polymerase I / RNA polymerase III complex / Formation of HIV elongation complex in the absence of HIV Tat / transcription by RNA polymerase I / RNA polymerase II, core complex / tRNA transcription by RNA polymerase III / RNA Polymerase II Transcription Elongation / Formation of RNA Pol II elongation complex / RNA Polymerase II Pre-transcription Events / embryo implantation / Inhibition of DNA recombination at telomere / mRNA Splicing - Major Pathway / cell surface receptor protein tyrosine kinase signaling pathway / TP53 Regulates Transcription of DNA Repair Genes / RNA Polymerase I Promoter Escape / Transcriptional regulation by small RNAs / Transcription-Coupled Nucleotide Excision Repair (TC-NER) / Formation of TC-NER Pre-Incision Complex / protein-DNA complex / NoRC negatively regulates rRNA expression / B-WICH complex positively regulates rRNA expression / Dual incision in TC-NER / Gap-filling DNA repair synthesis and ligation in TC-NER / ribonucleoside binding / Activation of anterior HOX genes in hindbrain development during early embryogenesis / fibrillar center / DNA-directed RNA polymerase / DNA-directed RNA polymerase activity / single-stranded DNA binding / chromosome / Estrogen-dependent gene expression / nucleic acid binding / transcription by RNA polymerase II / protein dimerization activity / protein stabilization / chromatin binding / chromatin / nucleolus / magnesium ion binding / mitochondrion / DNA binding / RNA binding / zinc ion binding / nucleoplasm / nucleus / cytosol / cytoplasm
Similarity search - Function
DNA-directed RNA polymerase I, subunit RPA34.5 / DNA-directed RNA polymerase I subunit RPA34.5 / RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor / Pol I subunit A12, C-terminal zinc ribbon / DNA-directed RNA polymerase I subunit RPA2, domain 4 / DNA-directed RNA pol I, largest subunit / : / RNA polymerase I, Rpa2 specific domain / DNA-directed RNA polymerases I and III subunit AC19 ...DNA-directed RNA polymerase I, subunit RPA34.5 / DNA-directed RNA polymerase I subunit RPA34.5 / RNA polymerase I associated factor, A49-like / A49-like RNA polymerase I associated factor / Pol I subunit A12, C-terminal zinc ribbon / DNA-directed RNA polymerase I subunit RPA2, domain 4 / DNA-directed RNA pol I, largest subunit / : / RNA polymerase I, Rpa2 specific domain / DNA-directed RNA polymerases I and III subunit AC19 / DNA-directed RNA polymerases I and III subunit AC40 / Zinc finger TFIIS-type signature. / DNA-directed RNA polymerase M, 15kDa subunit, conserved site / RNA polymerases M / 15 Kd subunits signature. / DNA-directed RNA polymerase subunit/transcription factor S / : / RNA polymerase, Rpb8 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / RNA polymerase Rpb8 / RNA polymerase subunit 8 / RNA polymerase, Rpb5, N-terminal / RNA polymerase Rpb5, N-terminal domain superfamily / RNA polymerase Rpb5, N-terminal domain / DNA-directed RNA polymerase, subunit RPB6 / DNA-directed RNA polymerase subunit RPABC5/Rpb10 / RNA polymerases, subunit N, zinc binding site / RNA polymerase subunit RPB10 / RNA polymerases N / 8 kDa subunit / RNA polymerases N / 8 Kd subunits signature. / DNA directed RNA polymerase, 7 kDa subunit / RNA polymerase archaeal subunit P/eukaryotic subunit RPABC4 / RNA polymerase, subunit H/Rpb5, conserved site / RNA polymerases H / 23 Kd subunits signature. / RNA polymerase subunit CX / DNA-directed RNA polymerase, 30-40kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo3/Rpb3/RPAC1 / RNA polymerases D / 30 to 40 Kd subunits signature. / DNA-directed RNA polymerase Rpb11, 13-16kDa subunit, conserved site / DNA-directed RNA polymerase subunit Rpo11 / RNA polymerases L / 13 to 16 Kd subunits signature. / RNA polymerase subunit RPABC4/transcription elongation factor Spt4 / Zinc finger, TFIIS-type / Transcription factor S-II (TFIIS) / Zinc finger TFIIS-type profile. / C2C2 Zinc finger / DNA-directed RNA polymerase, RBP11-like dimerisation domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerase, subunit H/Rpb5 C-terminal / DNA-directed RNA polymerase subunit Rpo5/Rpb5 / RPB5-like RNA polymerase subunit superfamily / RNA polymerase Rpb5, C-terminal domain / Archaeal Rpo6/eukaryotic RPB6 RNA polymerase subunit / DNA-directed RNA polymerase, 14-18kDa subunit, conserved site / RNA polymerases K / 14 to 18 Kd subunits signature. / DNA-directed RNA polymerase, subunit beta-prime / RNA polymerase Rpb6 / RNA polymerase, subunit omega/Rpo6/RPB6 / RNA polymerase Rpb6 / RNA polymerase Rpb2, domain 2 superfamily / RNA polymerase Rpb1, domain 3 superfamily / RPB6/omega subunit-like superfamily / DNA-directed RNA polymerase, insert domain / DNA-directed RNA polymerase, RpoA/D/Rpb3-type / RNA polymerase Rpb3/RpoA insert domain / RNA polymerase Rpb3/Rpb11 dimerisation domain / RNA polymerases D / RNA polymerase Rpb1, clamp domain superfamily / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 3 / RNA polymerase Rpb1, domain 1 / RNA polymerase, beta subunit, protrusion / RNA polymerase beta subunit / RNA polymerase Rpb1, domain 1 / RNA polymerase, alpha subunit / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / DNA-directed RNA polymerase, insert domain superfamily / RNA polymerase Rpb1, domain 2 / RNA polymerase Rpb1, domain 5 / RNA polymerase Rpb1, domain 4 / RNA polymerase Rpb2, domain 2 / RNA polymerase Rpb2, domain 2 / RNA polymerase, RBP11-like subunit / RNA polymerase, N-terminal / RNA polymerase Rpb1, funnel domain superfamily / RNA polymerase I subunit A N-terminus / RNA polymerase, beta subunit, conserved site / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerase Rpb2, OB-fold / RNA polymerase Rpb2, domain 7 / RNA polymerase Rpb2, domain 3 / RNA polymerases beta chain signature. / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain / DNA-directed RNA polymerase, subunit 2 / DNA-directed RNA polymerase, subunit 2, hybrid-binding domain superfamily / RNA polymerase Rpb2, domain 6 / Nucleic acid-binding, OB-fold
Similarity search - Domain/homology
DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA34 / DNA-directed RNA polymerase I subunit RPA1 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase I subunit RPA49 ...DNA-directed RNA polymerases I and III subunit RPAC1 / DNA-directed RNA polymerase I subunit RPA34 / DNA-directed RNA polymerase I subunit RPA1 / DNA-directed RNA polymerases I and III subunit RPAC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC1 / DNA-directed RNA polymerases I, II, and III subunit RPABC3 / DNA-directed RNA polymerases I, II, and III subunit RPABC4 / DNA-directed RNA polymerases I, II, and III subunit RPABC2 / DNA-directed RNA polymerases I, II, and III subunit RPABC5 / DNA-directed RNA polymerase I subunit RPA49 / DNA-directed RNA polymerase I subunit RPA2 / DNA-directed RNA polymerase I subunit RPA12
Similarity search - Component
Biological speciesHomo sapiens (human)
Methodsingle particle reconstruction / cryo EM / Resolution: 4.09 Å
AuthorsDaiss JL / Pilsl M / Straub K / Bleckmann A / Hoecherl M / Heiss FB / Abascal-Palacios G / Ramsay E / Tluckova K / Mars JC ...Daiss JL / Pilsl M / Straub K / Bleckmann A / Hoecherl M / Heiss FB / Abascal-Palacios G / Ramsay E / Tluckova K / Mars JC / Fuertges T / Bruckmann A / Rudack T / Bernecky C / Lamour V / Panov K / Vannini A / Moss T / Engel C
Funding support Germany, 2 items
OrganizationGrant numberCountry
German Research Foundation (DFG)EN 1204/1-1 Germany
German Research Foundation (DFG)CRC 960 Germany
CitationJournal: Life Sci Alliance / Year: 2022
Title: The human RNA polymerase I structure reveals an HMG-like docking domain specific to metazoans.
Authors: Julia L Daiß / Michael Pilsl / Kristina Straub / Andrea Bleckmann / Mona Höcherl / Florian B Heiss / Guillermo Abascal-Palacios / Ewan P Ramsay / Katarina Tlučková / Jean-Clement Mars / ...Authors: Julia L Daiß / Michael Pilsl / Kristina Straub / Andrea Bleckmann / Mona Höcherl / Florian B Heiss / Guillermo Abascal-Palacios / Ewan P Ramsay / Katarina Tlučková / Jean-Clement Mars / Torben Fürtges / Astrid Bruckmann / Till Rudack / Carrie Bernecky / Valérie Lamour / Konstantin Panov / Alessandro Vannini / Tom Moss / Christoph Engel /
Abstract: Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth, and dysregulation is observed in many cancer types. Here, we present the purification ...Transcription of the ribosomal RNA precursor by RNA polymerase (Pol) I is a major determinant of cellular growth, and dysregulation is observed in many cancer types. Here, we present the purification of human Pol I from cells carrying a genomic GFP fusion on the largest subunit allowing the structural and functional analysis of the enzyme across species. In contrast to yeast, human Pol I carries a single-subunit stalk, and in vitro transcription indicates a reduced proofreading activity. Determination of the human Pol I cryo-EM reconstruction in a close-to-native state rationalizes the effects of disease-associated mutations and uncovers an additional domain that is built into the sequence of Pol I subunit RPA1. This "dock II" domain resembles a truncated HMG box incapable of DNA binding which may serve as a downstream transcription factor-binding platform in metazoans. Biochemical analysis, in situ modelling, and ChIP data indicate that Topoisomerase 2a can be recruited to Pol I via the domain and cooperates with the HMG box domain-containing factor UBF. These adaptations of the metazoan Pol I transcription system may allow efficient release of positive DNA supercoils accumulating downstream of the transcription bubble.
History
DepositionJun 10, 2022-
Header (metadata) releaseAug 31, 2022-
Map releaseAug 31, 2022-
UpdateNov 20, 2024-
Current statusNov 20, 2024Processing site: PDBe / Status: Released

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Structure visualization

Supplemental images

emd_15135.png

Downloads & links

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Map

FileDownload / File: emd_15135.map.gz / Format: CCP4 / Size: 26.2 MB / Type: IMAGE STORED AS FLOATING POINT NUMBER (4 BYTES)
Projections & slices

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Size
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AxesZ (Sec.)Y (Row.)X (Col.)
1.51 Å/pix.
x 190 pix.
= 286.607 Å		1.51 Å/pix.
x 190 pix.
= 286.607 Å		1.51 Å/pix.
x 190 pix.
= 286.607 Å

Surface

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Images are generated by Spider.

Voxel sizeX=Y=Z: 1.50846 Å
Density

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Histogram (log scale)
Contour LevelBy AUTHOR: 0.0154
Minimum - Maximum-0.0588106 - 0.11714794
Average (Standard dev.)0.00056057016 (±0.0036750168)
SymmetrySpace group: 1
Details

EMDB XML:

Map geometry
Axis orderXYZ
Origin000
Dimensions190190190
Spacing190190190
CellA=B=C: 286.60742 Å
α=β=γ: 90.0 °

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Supplemental data

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Half map: #2

Fileemd_15135_half_map_1.map
Projections & Slices
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Half map: #1

Fileemd_15135_half_map_2.map
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Sample components

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Entire : RNA polymerase I

EntireName: RNA polymerase I
Components
  • Complex: RNA polymerase I
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA1
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA2
    • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC1
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC1
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC2
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC3
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA12
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC5
    • Protein or peptide: DNA-directed RNA polymerases I and III subunit RPAC2
    • Protein or peptide: DNA-directed RNA polymerases I, II, and III subunit RPABC4
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA49
    • Protein or peptide: DNA-directed RNA polymerase I subunit RPA34

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Supramolecule #1: RNA polymerase I

SupramoleculeName: RNA polymerase I / type: complex / ID: 1 / Parent: 0 / Macromolecule list: all
Source (natural)Organism: Homo sapiens (human)

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Macromolecule #1: DNA-directed RNA polymerase I subunit RPA1

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA1 / 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: 195.069047 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS KEVCSTCVQD FSNCSGHLGH IELPLTVYN PLLFDKLYLL LRGSCLNCHM LTCPRAVIHL LLCQLRVLEV GALQAVYELE RILNRFLEEN PDPSASEIRE E LEQYTTEI ...String:
MLISKNMPWR RLQGISFGMY SAEELKKLSV KSITNPRYLD SLGNPSANGL YDLALGPADS KEVCSTCVQD FSNCSGHLGH IELPLTVYN PLLFDKLYLL LRGSCLNCHM LTCPRAVIHL LLCQLRVLEV GALQAVYELE RILNRFLEEN PDPSASEIRE E LEQYTTEI VQNNLLGSQG AHVKNVCESK SKLIALFWKA HMNAKRCPHC KTGRSVVRKE HNSKLTITFP AMVHRTAGQK DS EPLGIEE AQIGKRGYLT PTSAREHLSA LWKNEGFFLN YLFSGMDDDG MESRFNPSVF FLDFLVVPPS RYRPVSRLGD QMF TNGQTV NLQAVMKDVV LIRKLLALMA QEQKLPEEVA TPTTDEEKDS LIAIDRSFLS TLPGQSLIDK LYNIWIRLQS HVNI VFDSE MDKLMMDKYP GIRQILEKKE GLFRKHMMGK RVDYAARSVI CPDMYINTNE IGIPMVFATK LTYPQPVTPW NVQEL RQAV INGPNVHPGA SMVINEDGSR TALSAVDMTQ REAVAKQLLT PATGAPKPQG TKIVCRHVKN GDILLLNRQP TLHRPS IQA HRARILPEEK VLRLHYANCK AYNADFDGDE MNAHFPQSEL GRAEAYVLAC TDQQYLVPKD GQPLAGLIQD HMVSGAS MT TRGCFFTREH YMELVYRGLT DKVGRVKLLS PSILKPFPLW TGKQVVSTLL INIIPEDHIP LNLSGKAKIT GKAWVKET P RSVPGFNPDS MCESQVIIRE GELLCGVLDK AHYGSSAYGL VHCCYEIYGG ETSGKVLTCL ARLFTAYLQL YRGFTLGVE DILVKPKADV KRQRIIEEST HCGPQAVRAA LNLPEAASYD EVRGKWQDAH LGKDQRDFNM IDLKFKEEVN HYSNEINKAC MPFGLHRQF PENSLQMMVQ SGAKGSTVNT MQISCLLGQI ELEGRRPPLM ASGKSLPCFE PYEFTPRAGG FVTGRFLTGI K PPEFFFHC MAGREGLVDT AVKTSRSGYL QRCIIKHLEG LVVQYDLTVR DSDGSVVQFL YGEDGLDIPK TQFLQPKQFP FL ASNYEVI MKSQHLHEVL SRADPKKALH HFRAIKKWQS KHPNTLLRRG AFLSYSQKIQ EAVKALKLES ENRNGRSPGT QEM LRMWYE LDEESRRKYQ KKAAACPDPS LSVWRPDIYF ASVSETFETK VDDYSQEWAA QTEKSYEKSE LSLDRLRTLL QLKW QRSLC EPGEAVGLLA AQSIGEPSTQ MTLNTFHFAG RGEMNVTLGI PRLREILMVA SANIKTPMMS VPVLNTKKAL KRVKS LKKQ LTRVCLGEVL QKIDVQESFC MEEKQNKFQV YQLRFQFLPH AYYQQEKCLR PEDILRFMET RFFKLLMESI KKKNNK ASA FRNVNTRRAT QRDLDNAGEL GRSRGEQEGD EEEEGHIVDA EAEEGDADAS DAKRKEKQEE EVDYESEEEE EREGEEN DD EDMQEERNPH REGARKTQEQ DEEVGLGTEE DPSLPALLTQ PRKPTHSQEP QGPEAMERRV QAVREIHPFI DDYQYDTE E SLWCQVTVKL PLMKINFDMS SLVVSLAHGA VIYATKGITR CLLNETTNNK NEKELVLNTE GINLPELFKY AEVLDLRRL YSNDIHAIAN TYGIEAALRV IEKEIKDVFA VYGIAVDPRH LSLVADYMCF EGVYKPLNRF GIRSNSSPLQ QMTFETSFQF LKQATMLGS HDELRSPSAC LVVGKVVRGG TGLFELKQPL R

UniProtKB: DNA-directed RNA polymerase I subunit RPA1

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Macromolecule #2: DNA-directed RNA polymerase I subunit RPA2

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA2 / type: protein_or_peptide / ID: 2 / Number of copies: 1 / Enantiomer: LEVO / EC number: DNA-directed RNA polymerase
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 128.379219 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA IPPFEFAFKD ERISFTILDA VISPPTVPK GTICKEANVY PAECRGRRST YRGKLTADIN WAVNGISKGI IKQFLGYVPI MVKSKLCNLR NLPPQALIEH H EEAEEMGG ...String:
MDPGSRWRNL PSGPSLKHLT DPSYGIPREQ QKAALQELTR AHVESFNYAV HEGLGLAVQA IPPFEFAFKD ERISFTILDA VISPPTVPK GTICKEANVY PAECRGRRST YRGKLTADIN WAVNGISKGI IKQFLGYVPI MVKSKLCNLR NLPPQALIEH H EEAEEMGG YFIINGIEKV IRMLIMPRRN FPIAMIRPKW KTRGPGYTQY GVSMHCVREE HSAVNMNLHY LENGTVMLNF IY RKELFFL PLGFALKALV SFSDYQIFQE LIKGKEDDSF LRNSVSQMLR IVMEEGCSTQ KQVLNYLGEC FRVKLNVPDW YPN EQAAEF LFNQCICIHL KSNTEKFYML CLMTRKLFAL AKGECMEDNP DSLVNQEVLT PGQLFLMFLK EKLEGWLVSI KIAF DKKAQ KTSVSMNTDN LMRIFTMGID LTKPFEYLFA TGNLRSKTGL GLLQDSGLCV VADKLNFIRY LSHFRCVHRG ADFAK MRTT TVRRLLPESW GFLCPVHTPD GEPCGLMNHL TAVCEVVTQF VYTASIPALL CNLGVTPIDG APHRSYSECY PVLLDG VMV GWVDKDLAPG IADSLRHFKV LREKRIPPWM EVVLIPMTGK PSLYPGLFLF TTPCRLVRPV QNLALGKEEL IGTMEQI FM NVAIFEDEVF AGVTTHQELF PHSLLSVIAN FIPFSDHNQS PRNMYQCQMG KQTMGFPLLT YQDRSDNKLY RLQTPQSP L VRPSMYDYYD MDNYPIGTNA IVAVISYTGY DMEDAMIVNK ASWERGFAHG SVYKSEFIDL SEKIKQGDSS LVFGIKPGD PRVLQKLDDD GLPFIGAKLQ YGDPYYSYLN LNTGESFVMY YKSKENCVVD NIKVCSNDTG SGKFKCVCIT MRVPRNPTIG DKFASRHGQ KGILSRLWPA EDMPFTESGM VPDILFNPHG FPSRMTIGML IESMAGKSAA LHGLCHDATP FIFSEENSAL E YFGEMLKA AGYNFYGTER LYSGISGLEL EADIFIGVVY YQRLRHMVSD KFQVRTTGAR DRVTNQPIGG RNVQGGIRFG EM ERDALLA HGTSFLLHDR LFNCSDRSVA HVCVKCGSLL SPLLEKPPPS WSAMRNRKYN CTLCSRSDTI DTVSVPYVFR YFV AELAAM NIKVKLDVV

UniProtKB: DNA-directed RNA polymerase I subunit RPA2

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Macromolecule #3: DNA-directed RNA polymerases I and III subunit RPAC1

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC1 / type: protein_or_peptide / ID: 3 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 39.301672 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS LEFDMVGIDA AIANAFRRIL LAEVPTMAV EKVLVYNNTS IVQDEILAHR LGLIPIHADP RLFEYRNQGD EEGTEIDTLQ FRLQVRCTRN PHAAKDSSDP N ELYVNHKV ...String:
MAASQAVEEM RSRVVLGEFG VRNVHTTDFP GNYSGYDDAW DQDRFEKNFR VDVVHMDENS LEFDMVGIDA AIANAFRRIL LAEVPTMAV EKVLVYNNTS IVQDEILAHR LGLIPIHADP RLFEYRNQGD EEGTEIDTLQ FRLQVRCTRN PHAAKDSSDP N ELYVNHKV YTRHMTWIPL GNQADLFPEG TIRPVHDDIL IAQLRPGQEI DLLMHCVKGI GKDHAKFSPV ATASYRLLPD IT LLEPVEG EAAEELSRCF SPGVIEVQEV QGKKVARVAN PRLDTFSREI FRNEKLKKVV RLARVRDHYI FSVESTGVLP PDV LVSEAI KVLMGKCRRF LDELDAVQMD

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC1

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Macromolecule #4: DNA-directed RNA polymerases I, II, and III subunit RPABC1

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC1
type: protein_or_peptide / ID: 4 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 24.584223 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN ...String:
MDDEEETYRL WKIRKTIMQL CHDRGYLVTQ DELDQTLEEF KAQSGDKPSE GRPRRTDLTV LVAHNDDPTD QMFVFFPEEP KVGIKTIKV YCQRMQEENI TRALIVVQQG MTPSAKQSLV DMAPKYILEQ FLQQELLINI TEHELVPEHV VMTKEEVTEL L ARYKLREN QLPRIQAGDP VARYFGIKRG QVVKIIRPSE TAGRYITYRL VQ

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC1

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Macromolecule #5: DNA-directed RNA polymerases I, II, and III subunit RPABC2

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC2
type: protein_or_peptide / ID: 5 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 14.491026 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MSDNEDNFDG DDFDDVEEDE GLDDLENAEE EGQENVEILP SGERPQANQK RITTPYMTKY ERARVLGTRA LQIAMCAPVM VELEGETDP LLIAMKELKA RKIPIIIRRY LPDGSYEDWG VDELIITD

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC2

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Macromolecule #6: DNA-directed RNA polymerases I, II, and III subunit RPABC3

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC3
type: protein_or_peptide / ID: 6 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 17.162273 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MAGILFEDIF DVKDIDPEGK KFDRVSRLHC ESESFKMDLI LDVNIQIYPV DLGDKFRLVI ASTLYEDGTL DDGEYNPTDD RPSRADQFE YVMYGKVYRI EGDETSTEAA TRLSAYVSYG GLLMRLQGDA NNLHGFEVDS RVYLLMKKLA F

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC3

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Macromolecule #7: DNA-directed RNA polymerase I subunit RPA12

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA12 / type: protein_or_peptide / ID: 7 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 13.917695 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MSVMDLANTC SSFQSDLDFC SDCGSVLPLP GAQDTVTCIR CGFNINVRDF EGKVVKTSVV FHQLGTAMPM SVEEGPECQG PVVDRRCPR CGHEGMAYHT RQMRSADEGQ TVFYTCTNCK FQEKEDS

UniProtKB: DNA-directed RNA polymerase I subunit RPA12

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Macromolecule #8: DNA-directed RNA polymerases I, II, and III subunit RPABC5

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC5
type: protein_or_peptide / ID: 8 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.655123 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MIIPVRCFTC GKIVGNKWEA YLGLLQAEYT EGDALDALGL KRYCCRRMLL AHVDLIEKLL NYAPLEK

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC5

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Macromolecule #9: DNA-directed RNA polymerases I and III subunit RPAC2

MacromoleculeName: DNA-directed RNA polymerases I and III subunit RPAC2 / type: protein_or_peptide / ID: 9 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 15.259222 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MEEDQELERK ISGLKTSMAE GERKTALEMV QAAGTDRHCV TFVLHEEDHT LGNSLRYMIM KNPEVEFCGY TTTHPSESKI NLRIQTRGT LPAVEPFQRG LNELMNVCQH VLDKFEASIK DYKDQKASRN ESTF

UniProtKB: DNA-directed RNA polymerases I and III subunit RPAC2

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Macromolecule #10: DNA-directed RNA polymerases I, II, and III subunit RPABC4

MacromoleculeName: DNA-directed RNA polymerases I, II, and III subunit RPABC4
type: protein_or_peptide / ID: 10 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 7.018244 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString:
MDTQKDVQPP KQQPMIYICG ECHTENEIKS RDPIRCRECG YRIMYKKRTK RLVVFDAR

UniProtKB: DNA-directed RNA polymerases I, II, and III subunit RPABC4

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Macromolecule #11: DNA-directed RNA polymerase I subunit RPA49

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA49 / type: protein_or_peptide / ID: 11 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 47.330234 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MAAEVLPSAR WQYCGAPDGS QRAVLVQFSN GKLQSPGNMR FTLYENKDST NPRKRNQRIL AAETDRLSYV GNNFGTGALK CNTLCRHFV GILNKTSGQM EVYDAELFNM QPLFSDVSVE SELALESQTK TYREKMDSCI EAFGTTKQKR ALNTRRMNRV G NESLNRAV ...String:
MAAEVLPSAR WQYCGAPDGS QRAVLVQFSN GKLQSPGNMR FTLYENKDST NPRKRNQRIL AAETDRLSYV GNNFGTGALK CNTLCRHFV GILNKTSGQM EVYDAELFNM QPLFSDVSVE SELALESQTK TYREKMDSCI EAFGTTKQKR ALNTRRMNRV G NESLNRAV AKAAETIIDT KGVTALVSDA IHNDLQDDSL YLPPCYDDAA KPEDVYKFED LLSPAEYEAL QSPSEAFRNV TS EEILKMI EENSHCTFVI EALKSLPSDV ESRDRQARCI WFLDTLIKFR AHRVVKRKSA LGPGVPHIIN TKLLKHFTCL TYN NGRLRN LISDSMKAKI TAYVIILALH IHDFQIDLTV LQRDLKLSEK RMMEIAKAMR LKISKRRVSV AAGSEEDHKL GTLS LPLPP AQTSDRLAKR RKIT

UniProtKB: DNA-directed RNA polymerase I subunit RPA49

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Macromolecule #12: DNA-directed RNA polymerase I subunit RPA34

MacromoleculeName: DNA-directed RNA polymerase I subunit RPA34 / type: protein_or_peptide / ID: 12 / Number of copies: 1 / Enantiomer: LEVO
Source (natural)Organism: Homo sapiens (human)
Molecular weightTheoretical: 55.065523 KDa
Recombinant expressionOrganism: Homo sapiens (human)
SequenceString: MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH VPLSGSQIVK GKLAGKRHRY RVLSSCPQA GEATLLAPST EAGGGLTCAS APQGTLRILE GPQQSLSGSP LQPIPASPPP QIPPGLRPRF CAFGGNPPVT G PRSALAPN ...String:
MEEPQAGDAA RFSCPPNFTA KPPASESPRF SLEALTGPDT ELWLIQAPAD FAPECFNGRH VPLSGSQIVK GKLAGKRHRY RVLSSCPQA GEATLLAPST EAGGGLTCAS APQGTLRILE GPQQSLSGSP LQPIPASPPP QIPPGLRPRF CAFGGNPPVT G PRSALAPN LLTSGKKKKE MQVTEAPVTQ EAVNGHGALE VDMALGSPEM DVRKKKKKKN QQLKEPEAAG PVGTEPTVET LE PLGVLFP STTKKRKKPK GKETFEPEDK TVKQEQINTE PLEDTVLSPT KKRKRQKGTE GMEPEEGVTV ESQPQVKVEP LEE AIPLPP TKKRKKEKGQ MAMMEPGTEA MEPVEPEMKP LESPGGTMAP QQPEGAKPQA QAALAAPKKK TKKEKQQDAT VEPE TEVVG PELPDDLEPQ AAPTSTKKKK KKKERGHTVT EPIQPLEPEL PGEGQPEARA TPGSTKKRKK QSQESRMPET VPQEE MPGP PLNSESGEEA PTGRDKKRKQ QQQQPV

UniProtKB: DNA-directed RNA polymerase I subunit RPA34

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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

BufferpH: 7.8
VitrificationCryogen name: ETHANE

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Electron microscopy

MicroscopeJEOL CRYO ARM 200
Image recordingFilm or detector model: GATAN K2 SUMMIT (4k x 4k) / Average electron dose: 40.0 e/Å2
Electron beamAcceleration voltage: 200 kV / Electron source: FIELD EMISSION GUN
Electron opticsIllumination mode: FLOOD BEAM / Imaging mode: BRIGHT FIELD / Nominal defocus max: 2.7 µm / Nominal defocus min: 1.2 µm

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Image processing

Startup modelType of model: PDB ENTRY
PDB model - PDB ID:

4c2m

Final reconstructionResolution.type: BY AUTHOR / Resolution: 4.09 Å / Resolution method: FSC 0.143 CUT-OFF / Number images used: 108012
Initial angle assignmentType: ANGULAR RECONSTITUTION
Final angle assignmentType: ANGULAR RECONSTITUTION

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