Vadim Molodtsov


Affiliation: Pennsylvania State University
Country: USA


  1. Murakami K, Davydova E, Rothman Denes L. X-ray crystal structure of the polymerase domain of the bacteriophage N4 virion RNA polymerase. Proc Natl Acad Sci U S A. 2008;105:5046-51 pubmed publisher
  2. Murakami K, Shin Y, Turnbough C, Molodtsov V. X-ray crystal structure of a reiterative transcription complex reveals an atypical RNA extension pathway. Proc Natl Acad Sci U S A. 2017;114:8211-8216 pubmed publisher
    ..Nascent transcripts containing reiteratively added G residues are eventually extended by nonreiterative transcription, revealing an atypical pathway for the formation of a transcription elongation complex. ..
  3. Mosaei H, Molodtsov V, Kepplinger B, Harbottle J, Moon C, Jeeves R, et al. Mode of Action of Kanglemycin A, an Ansamycin Natural Product that Is Active against Rifampicin-Resistant Mycobacterium tuberculosis. Mol Cell. 2018;72:263-274.e5 pubmed publisher
    ..Previous ansa-chain modifications in the rifamycin series have proven unsuccessful. Thus, KglA represents a key starting point for the development of a new class of ansa-chain derivatized ansamycins to tackle rifampicin resistance. ..
  4. Molodtsov V, Murakami K. Minimalism and functionality: Structural lessons from the heterodimeric N4 bacteriophage RNA polymerase II. J Biol Chem. 2018;293:13616-13625 pubmed publisher
    ..This work establishes a structural basis for studying mechanistic aspects of transcription by factor-dependent minimum RNAP. ..
  5. Murakami K. Structural biology of bacterial RNA polymerase. Biomolecules. 2015;5:848-64 pubmed publisher
  6. Narayanan A, Vago F, Li K, Qayyum M, Yernool D, Jiang W, et al. Cryo-EM structure of Escherichia coli ?70 RNA polymerase and promoter DNA complex revealed a role of ? non-conserved region during the open complex formation. J Biol Chem. 2018;293:7367-7375 pubmed publisher
    ..We propose that the ?NCR and DNA interaction is conserved in proteobacteria, and RNAP in other bacteria replaces its role with a transcription factor. ..
  7. Bruhn Olszewska B, Molodtsov V, Sobala M, Dylewski M, Murakami K, Cashel M, et al. Structure-function comparisons of (p)ppApp vs (p)ppGpp for Escherichia coli RNA polymerase binding sites and for rrnB P1 promoter regulatory responses in vitro. Biochim Biophys Acta Gene Regul Mech. 2018;1861:731-742 pubmed publisher
    ..Our observations underscore the importance of the (p)ppNpp's purine nucleobase for interactions with RNAP, which may lead to a better fundamental understanding of (p)ppGpp regulation of RNAP activity. ..
  8. Molodtsov V, Sineva E, Zhang L, Huang X, Cashel M, Ades S, et al. Allosteric Effector ppGpp Potentiates the Inhibition of Transcript Initiation by DksA. Mol Cell. 2018;69:828-839.e5 pubmed publisher
    ..This work establishes a structural basis for understanding the pleiotropic effects of DksA and ppGpp on transcriptional regulation in proteobacteria. ..
  9. Murakami K. X-ray crystal structure of Escherichia coli RNA polymerase ?70 holoenzyme. J Biol Chem. 2013;288:9126-34 pubmed publisher
    ..E. coli RNAP crystals can be prepared from a convenient overexpression system, allowing further structural studies of bacterial RNAP mutants, including functionally deficient and antibiotic-resistant RNAPs...

More Information


  1. Basu R, Warner B, Molodtsov V, Pupov D, Esyunina D, Fern ndez Tornero C, et al. Structural basis of transcription initiation by bacterial RNA polymerase holoenzyme. J Biol Chem. 2014;289:24549-59 pubmed publisher
    ..Given the structural conservation of the RNAP active site, the mechanism of de novo RNA priming appears to be conserved in all cellular RNAPs...