Ph.D. - University of Turku, Dept. of Biochemistry, Finland, 2005

Postdoc - Ohio State Univesity, Dept. of Microbiology, USA, 2006-2009

Principal investigator - University of Turku, Dept. of Biochemistry, Finland, 2009-2020

Principal investigator - University of Turku, Dept. of Life Technologies, Finland, 2020-


Georgi A. Belogurov, Ph.D., Associate Professor

Research interests

Transcription, nucleic acids enzymes, enzyme kinetics, protein chemistry, molecular modeling, nucleoside analogue inhibitors, phylogenomics.


Google Scholar profile


University of Turku, Dept. of Life Technologies, Tykistökatu 6, 20520 Turku, Finland. E-mail: gebelo(at)


Computational and Molecular Methodologies for Life Sciences – CompLifeSci

Sigrid Jusélius Foundation Senior Researcher 2020 – 2023

Turku Collegium for Science and Medicine – TCSM 2009 –


MULTISUBUNIT RNA POLYMERASE: Molecular Mechanisms of Transcription (RNAP group homepage)


Huang Y.H., Trapp V., Puro O., Mäkinen J.J., Metsä-Ketelä M., Wahl M.C., Belogurov G.A. (2022) Fluorogenic RNA aptamers to probe transcription initiation and co-transcriptional RNA folding by multi-subunit RNA polymerases. Methods Enzymol. 675:207-233. [PubMed].

Rosenqvist P., Mäkinen J.J., Palmu K., Jokinen J., Prajapati R.K., Korhonen H.J., Virta P., Belogurov G.A., Metsä-Ketelä M. (2022) The role of the maleimide ring system on the structure-activity relationship of showdomycin. Eur. J. Med. Chem. 237:114342. [PubMed].

Malinen A.M., Bakermans J., Aalto-Setälä E., Blessing M., Bauer D.L.V., Parilova O., Belogurov G.A., Dulin D., Kapanidis A.N. (2022) Real-Time Single-Molecule Studies of RNA Polymerase-Promoter Open Complex Formation Reveal Substantial Heterogeneity Along the Promoter-Opening Pathway. J. Mol. Biol. 434(2):167383. [PubMed].

Mäkinen J.J., Shin Y., Vieras E., Virta P., Metsä-Ketelä M., Murakami K.S., Belogurov G.A. (2021) The mechanism of the nucleo-sugar selection by multi-subunit RNA polymerases. Nat. Commun. 12:796. [PubMed].

    Figure 5 in 3D (WebGL in browser):   Panel AB     Panel C     Panel D
    Figure 6 in 3D (WebGL in browser):   Panel A       Panel B
    Figure 7 in 3D (WebGL in browser):   Panel AB     Panel C     Panel D

Said N., Hilal T., Sunday N.D., Khatri A, Bürger J., Mielke T., Belogurov G.A., Loll B., Sen R., Artsimovitch I., Wahl M.C. (2021) Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase Rho. Science 371(6524):eabd1673. [PubMed]

Pei H.-H., Hilal T., Chen Z.A., Huang Y.-H., Gao Y., Said N., Loll B., Rappsilber J., Belogurov G.A., Artsimovitch I., Wahl M.C. (2020) The delta subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling. Nat. Commun. 11(1):6418. [PubMed].

    Monomeric RNAP-HelD complex in 3D (WebGL in browser):   Overview
    Dimeric RNAP-HelD complex in 3D (WebGL in browser):   Overview
    RNAP-HelD superimposition with EC in 3D (WebGL in browser):   Overview

Agapov A., Ignatov A., Turtola M., Belogurov G., Esyunina D., Kulbachinskiy A. (2020) Role of the trigger loop in translesion RNA synthesis by bacterial RNA polymerase. J. Biol. Chem. 295(28):9583-9595. [PubMed]

Prajapati R.K., Rosenqvist P., Palmu K., Mäkinen J.J., Malinen A.M., Virta P., Metsä-Ketelä M., Belogurov G.A. (2019) Oxazinomycin arrests RNA polymerase at the polythymidine sequences. Nucleic Acids Res. 47(19):10296-10312. [PubMed]

Belogurov G.A., Artsimovitch I. (2019) The mechanisms of substrate selection, catalysis and translocation by the elongating RNA polymerase. J. Mol. Biol. 431(20):3975-4006. [PubMed]

Rosenqvist P, Palmu K, Prajapati R.K., Yamada K., Niemi J., Belogurov G.A., Metsä-Ketelä M., Virta P. (2019) Characterization of C-nucleoside Antimicrobials from Streptomyces albus DSM 40763: Strepturidin is Pseudouridimycin Sci. Rep. 9(1):8935. [PubMed]

Turtola M., Mäkinen J.J., Belogurov G.A. (2018) Active site closure stabilizes the backtracked state of RNA polymerase. Nucleic Acids Res. 46(20):10870-10887. [PubMed]

    Supplementary Figure S6 in 3D (WebGL in browser):  Option 1   Option 2

Sanz-Murillo M., Xu J., Belogurov G.A., Calvo O., Gil-Carton D., Moreno-Morcillo M., Wang D., Fernández-Tornero C. (2018) Structural basis of RNA polymerase I stalling at UV light-induced DNA damage. Proc. Natl. Acad. Sci. USA 115(36):8972-8977. [PubMed]

Nedialkov Y., Svetlov D., Belogurov G.A., Artsimovitch I. (2018) Locking the non-template DNA to control transcription. Mol. Microbiol. 109(4):445-457. [PubMed]

    Figure 4 in 3D (WebGL in browser):   Model 1     Model 2     Model 3     Model 4

Artsimovitch I., Belogurov G.A. (2018) Uneven braking spins RNA Polymerase into a pause. Mol. Cell 69(5):723-725. [PubMed]

    Animated Figure 1 (GIF)

Palmu K., Rosenqvist P., Thapa K., Ilina Y., Siitonen V., Baral B., Mäkinen J., Belogurov G., Virta P., Niemi J., Metsä-Ketelä M. (2017) Discovery of the Showdomycin Gene Cluster from Streptomyces showdoensis ATCC 15227 Yields Insight into the Biosynthetic Logic of C-Nucleoside Antibiotics. ACS Chem. Biol. 12(6):1472-1477. [PubMed]

NandyMazumdar M., Nedialkov Y., Svetlov D., Sevostyanova A., Belogurov G.A., Artsimovitch I. (2016) RNA polymerase gate loop guides the nontemplate DNA strand in transcription complexes. Proc. Natl. Acad. Sci. USA 113(52):14994-14999. [PubMed]

    Figure 1 in 3D (WebGL in browser):   panel A     panel B

Turtola M., Belogurov G.A., (2016) NusG inhibits RNA polymerase backtracking by stabilizing the minimal transcription bubble. eLife 5. pii: e18096. [PubMed]

    Figure 8 in 3D (WebGL in browser):   Panel C

Maddalena L.L., Niederholtmeyer H., Turtola M., Swank Z.N., Belogurov G.A., Maerkl S.J. (2016) GreA and GreB enhance expression of Escherichia coli RNA polymerase promoters in a reconstituted transcription-translation system. ACS Synth. Biol. 5(9):929-35. [PubMed]

Esyunina D., Turtola M., Pupov D., Bass I., Klimašauskas S., Belogurov G., Kulbachinskiy A. (2016) Lineage-specific variations in the trigger loop modulate RNA proofreading by bacterial RNA polymerases. Nucleic Acids Res. 44(3):1298-308.[PubMed]

Belogurov G.A., Artsimovitch I. (2015) Regulation of Transcript Elongation. Annu. Rev. Microbiol. 69: 49-69. [PubMed]

Artsimovitch I., Belogurov G.A. (2015) Creative Math of RNA Polymerase III Termination: Sense Plus Antisense Makes More Sense. Mol. Cell 58(6):974-6. [PubMed]

Malinen A.M., Turtola M., Belogurov G.A. (2015) Monitoring translocation of multisubunit RNA polymerase along the DNA with fluorescent base analogues. Methods Mol. Biol. 1276:31-51. [PubMed]

Malinen A.M., NandyMazumdar M., Turtola M., Malmi H., Grocholski T., Artsimovitch I., Belogurov G.A. (2014) CBR antimicrobials alter coupling between the bridge helix and the ß subunit in RNA polymerase. Nat. Commun. 5:3408 doi: 10.1038/ncomms4408. [PubMed]

Kallio P., Patrikainen P., Belogurov G.A., Mäntsälä P., Yang K., Niemi J., Metsä-Ketelä M. (2013) Tracing the evolution of angucyclinone monooxygenases: structural determinants for C-12b hydroxylation and substrate inhibition in PgaE. Biochemistry 52(26):4507-16. [PubMed]

Malinen A.M., Turtola M., Parthiban M., Vainonen L., Johnson M.S., Belogurov G.A. (2012) Active site opening and closure control translocation of multisubunit RNA polymerase. Nucleic Acids Res. 40(15): 7442-51. [PubMed]

Sevostyanova A., Belogurov G.A., Mooney R.A., Landick R., Artsimovitch I. (2011) The ß subunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol. Cell 43(2): 253-262. [PubMed]

Luoto H.H., Belogurov G.A., Baykov A.A., Lahti R., Malinen A.M. (2011) Na+-translocating membrane pyrophosphatases are widespread in the microbial world and evolutionarily precede H+-translocating pyrophosphatases. J. Biol. Chem. 286(24): 21633-42 [PubMed]

Belogurov G.A., Sevostyanova A., Svetlov V., Artsimovitch I. (2010). Functional regions of the N-terminal domain of the antiterminator RfaH. Mol. Microbiol. 76 (2): 286-301 [PubMed]

Belogurov, G.A., Mooney, R.A. Svetlov, V., Landick, R., Artsimovitch, I. (2009) Functional specialization of transcription elongation factors. EMBO J. 28(2):112-22 [PubMed]

Belogurov, G.A., Vassylyeva, M.N. Sevostyanova, A., Xiang, A., Lira, R., Webber, S., Klyuyev, S., Nudler, E., Artsimovitch, I., Vassylyev, D.G. (2009) Transcription inactivation through local refolding of the RNA polymerase structure. Nature 457(7227): 332-335 [PubMed]

Svetlov V., Belogurov G.A., Shabrova E., Vassylyev D.G., Artsimovitch I. (2007) Allosteric control of the RNA polymerase by the elongation factor RfaH. Nucleic Acids Res. 35(17):5694-705 [PubMed]

Jämsen J., Tuominen H., Salminen A., Belogurov G.A., Magretova N.N., Baykov A.A., Lahti R. (2007) A CBS domain-containing pyrophosphatase of Moorella thermoacetica is regulated by adenine nucleotides. Biochem J. 408(3):327-33 [PubMed]

Belogurov G.A., Vassylyeva M.N., Svetlov V., Klyuyev S., Grishin N.V., Vassylyev D.G., Artsimovitch I. (2007) Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Mol Cell. 26(1):117-29 [PubMed]

Malinen A. M., Belogurov G. A., Baykov A. A., Lahti R. (2007) Na+-pyrophosphatase: a novel primary sodium pump.
Biochemistry 46(30):8872-8 [PubMed]

Belogurov, G. A., Malinen, A. M., Turkina, M. V., Jalonen, U., Rytkönen, K., Baykov, A. A., Lahti, R. (2005) Membrane-bound pyrophosphatase of
Thermotoga maritima requires sodium for activity. Biochemistry 44(6): 2088-2096 [PubMed]

Malinen, A. M., Belogurov, G. A., Salminen, M., Baykov, A. A. and Lahti, R. (2004) Elucidating the role of conserved glutamates in H+-pyrophosphatase of
Rhodospirillum rubrum. J. Biol. Chem. 279: 26811-26816 [PubMed]

Belogurov, G. A. and Lahti, R. (2002) A Lysine substitute for K+: A460K mutation eliminates K+-dependence in H+-pyrophosphatase of
Carboxydothermus hydrogenoformans. J. Biol. Chem. 277: 49651-49654 [PubMed]

Belogurov, G. A., Turkina, M. V., Penttinen, A., Huopalahti, S., Baykov, A. A. and Lahti, R. (2002) H+-Pyrophosphatase of
Rhodospirillum rubrum: High-yield expression in Escherichia coli and identification of the Cys residues responsible for inactivation by mersalyl. J. Biol. Chem. 277: 22209-22214 [PubMed]

Belogurov G. A., Fabrichniy I. P., Pohjanjoki P., Kasho V. N., Lehtihuhta E., Turkina M. V., Cooperman B. S., Goldman A., Baykov A.A., Lahti R. (2000) Catalytically important ionizations along the reaction pathway of yeast pyrophosphatase.
Biochemistry 39(45):13931-13938 [PubMed]