Affiliations

• Center for RNA Biology
• Ohio State Biochemistry Program
• Molecular, Cellular and Developmental Biology Program

 

Awards

• Doctor Honoris Causa, University of Turku-Finland
• Fellow, American Association for the Advancement of Science
• Fellow, American Academy of Microbiology

 

Research Interests

We study RNA chain synthesis by multi-subunit RNA polymerases, focusing on enzymes from bacteria, such as Escherichia coli and Bacillus subtilis, and viruses, such as SARS-CoV-2. We use a combination of biochemical, biophysical, computational, and genetic approaches to elucidate the mechanism of catalysis, to understand how accessory protein factors modulate RNA polymerase progression through the transcription cycle, and to identify small molecules that can be developed into novel antibacterials and antivirals. We also investigate crosstalk between transcription and concurrent processes, such as translation, the nascent RNA folding, and DNA repair.

 

Recent Publications

Pei H-H, Hilal T, Chen Z, Huang Y-H, Said N, Gao Y, Loll B, Rappsilber Y, Belogurov GA, Artsimovitch I, Wahl MC (2020) The δ subunit and NTPase HelD institute a two-pronged mechanism for RNA polymerase recycling. Nat Commun., in press.

Said N, Hilal T, Sunday ND, Khatri A, Bürger J, Mielke T, Loll B, Sen R, Belogurov GA, Artsimovitch I, Wahl MC (2020) Steps toward translocation-independent RNA polymerase inactivation by terminator ATPase ρ. Science, 26 Nov 2020: eabd1673.

Wang B, Gumerov VM, Andrianova EP, Zhulin IB, Artsimovitch I (2020) Origins and molecular evolution of the NusG paralog RfaH. mBio, 11: p. e02717-20.

Galaz-Davison P, Molina J, Silletti S, Komives E, Knauer SH, Artsimovitch I, Ramirez-Sarmiento C (2020) Differential local stability governs the metamorphic fold-switch of bacterial virulence factor RfaH. Biophys J, 118(1), 96-104. 

Bergkessel M, Babin BM, VanderVelde D, Sweredoski MJ, Moradian A, Eggleston-Rangel R, Hess S, Tirrell DA, Artsimovitch I, Newman DK (2019) The dormancy-specific regulator, SutA, is intrinsically disordered and modulates transcription initiation in Pseudomonas aeruginosa. Mol Microbiol. 112(3), 992-1009. 

Zuber PK, Schgweimer K, Rösch P, Artsimovitch I, Knauer SH (2019) Reversible fold-switching of the antitermination factor RfaH. Nat Commun., 10, 702. 

Svetlov D, Shi D, Twentyman J, Nedialkov Y, Rosen DA, Abagyan R, Artsimovitch I (2018) In silico discovery of small molecules that inhibit RfaH recruitment to RNA polymerase. Mol Microbiol. doi: 10.1111/mmi.14093.

Nedialkov Y, Svetlov D, Belogurov GA, Artsimovitch I (2018) Locking the non-template DNA to control transcription. Mol Microbiol. 109, 445-457.

Shi D, Svetlov D, Abagyan R, Artsimovitch I (2017) Flipping states: a few key residues decide the winning conformation of the only universally conserved transcription factor. Nucleic Acids Res. 45, 8835-8843.

Other relevant publications

Widom JR, Nedialkov YA, Rai V, Hayes RL, Brooks CL III, Artsimovitch I, Walter NG (2018) Ligand modulates cross-coupling between riboswitch folding and transcriptional pausing. Mol Cell, 72(3), 541-52. 

NandyMazumdar M, Nedialkov Y, Svetlov D, Sevostyanova A, Belogurov GA, Artsimovitch I (2016) RNA polymerase gate loop guides the nontemplate DNA strand in transcription complexes. Proc Natl Acad Sci U S A. 113, 14994-14999.

Burmann BM, Knauer SH, Sevostyanova A, Schweimer K, Mooney RA, Landick R, Artsimovitch I, Rösch P (2012) An α-helix to β-barrel domain switch transforms the transcription factor RfaH into a translation factor. Cell, 150, 291-303.

Sevostyanova A, Belogurov GA, Mooney RA, Landick R, Artsimovitch I (2011) The beta subunit gate loop is required for RNA polymerase modification by RfaH and NusG. Mol Cell. 43, 253-62.

Belogurov GA, Vassylyeva MN, Sevostyanova A, Appleman JR, Xiang AX, Lira R, Webber SE, Klyuyev S, Nudler E, Artsimovitch I, Vassylyev DG (2009) Transcription inactivation through local refolding of the RNA polymerase structure. Nature. 457, 332-5.

Belogurov GA, Mooney RA, Svetlov V, Landick R, Artsimovitch I (2009) Functional specialization of transcription elongation factors. EMBO J. 28, 112-22.

Sevostyanova A, Svetlov V, Vassylyev DG, Artsimovitch I (2008) The elongation factor RfaH and the initiation factor sigma bind to the same site on the transcription elongation complex. Proc Natl Acad Sci U S A. 105, 865-70.

Vassylyev DG, Vassylyeva MN, Perederina A, Tahirov TH, Artsimovitch I (2007) Structural basis for transcription elongation by bacterial RNA polymerase. Nature. 448, 157-62.

Belogurov GA, Vassylyeva MN, Svetlov V, Klyuyev S, Grishin NV, Vassylyev DG, Artsimovitch I (2007) Structural basis for converting a general transcription factor into an operon-specific virulence regulator. Mol Cell. 26, 117-29.

Vassylyev DG, Svetlov V, Vassylyeva MN, Perederina A, Igarashi N, Matsugaki N, Wakatsuki S, Artsimovitch I (2005) Structural basis for transcription inhibition by tagetitoxin. Nat Struct Mol Biol. 12, 1086-93.