Faculté de médecine Faculté de médecine

Olesya Panasenko

Photo
Dr Olesya Panasenko

Scientific Supervision and Administration of BioCode: R2P Core Facility

D09.2152.A (CMU Building D – 9th floor)
+41 22 379 54 84
E-mail

I am a biochemist with over 25 years of experience in scientific research, focusing on protein biochemistry, protein translation, co-translational quality control, protein folding, and degradation.

I currently lead the R2P Platform, which specializes in Ribo-Seq, polysome fractionation, in vitro translation, co-translational quality control, and related techniques.

Publications

  1. Collart M.A., Panasenko O.O., (2025), Assembly in action: Protein structure orchestrates assembly pathway, and intertwining defines co-translational assembly, Molecular Cell, 85, 466
  2. Cherkaoui S., Yang L., McBride M., Turn C.S., Lu W., Eigenmann C., Allen G.E., Panasenko O.O., Zhang L., Vu A., Liu K., Li Y., Gandhi O.H., Surrey L., Wierer M., White E., Rabinowitz J.D., Hogarty M.D., Morscher R.J. (2024), Reprogramming neuroblastoma by diet-enhanced polyamine depletion, bioRxiv preprint
  3. Maiti S., Bhattacharya K., Wider D., Hany D., Panasenko O., Bernasconi L., Hulo N., Picard D. (2023), Hsf1 and the molecular chaperone Hsp90 support a "rewiring stress response" leading to an adaptive cell size increase in chronic stress, eLife, 12, RP8865
  4. Dohnalkova M., Krasnykov K., Mendel M., Li L., Panasenko O.O.,  Fleury-Olela F., Broberg Vågbø C., Homolka D., Pillai R.S., (2023) Essential roles of RNA cap-proximal ribose methylation in mammalian embryonic development and fertility. Cell Reports, 42, 112786
  5. Chen S., Allen G.E., Panasenko O.O., Collart M.A. (2023) Not4-dependent targeting of MMF1 mRNA to mitochondria limits its expression via ribosome pausing, Egd1 ubiquitination, Caf130, No-Go-Decay and autophagy. BioRxiv, Nucleic Acids Research, 51, 5022.
  6. Allen G.E., Weiss B., Panasenko O.O., Huch S., Villanyi Z., Albert B., Dilg D., Zagatti M., Schaughency P., Liao S.E., Corden J., Polte C., Shore D., Ignatova Z., Pelechano V., Collart M.A. (2023), Not1 and Not4 inversely determine mRNA solubility that sets the dynamics of co-translational events. Genome Biology, 24, 30
  7. Allen G.E., Panasenko O.O., Villanyi Z., Zagatti M., Weiss B., Pagliazzo L., Huch S., Polte C., Zahoran Z., Hughes C.S., Pelechano V., Ignatova Z., Collart M.A. (2021) Not4 and Not5 modulate translation elongation by Rps7A ubiquitination, Rli1 moonlighting, and condensates that exclude eIF5A. Cell Reports. 36, 109633
  8. Bezrukov F., Prados J., Renzoni A. Panasenko O.O. (2021) MazF toxin causes alterations in Staphylococcus aureus transcriptome, translatome and proteome that underlie bacterial dormancy. Nucleic Acids Research, 49, 2085
  9. Sierra R., Prados J., Panasenko O.O., Andrey D.O., Baldi A., Fleuchot B., Redder P., Kelley W.L., Viollier P., Renzoni A. (2020) Insights into the global effect on Staphylococcus aureus growth arrest by induction of the endoribonuclease MazF toxin. Nucleic Acids Research, 48, 8545
  10. Panasenko O.O., Bezrukov F., Komarynets O., Renzoni A. (2020) YjbH Solubility Controls Spx in Staphylococcus aureus: Implication for MazEF Toxin-Antitoxin System Regulation Frontiers in Microbiology, 11, 113
  11. Ramadori G., Ioris R.M., Villanyi Z., Firnkes R., Panasenko O.O., Allen G., Konstantinidou G, Aras E., Brenachot X., Biscotti T., Charollais A., Luchetti M., Bezrukov F., Santinelli A., Samad M., Baldi P., Collart M.A., Coppari R. (2020) FKBP10 Regulates Protein Translation to Sustain Lung Cancer Growth, Cell Reports, 30, 3851
  12. Allen G.E., Panasenko O.O., Villanyi Z., Zagatti M., Weiss B., Polte C., Ignatova Z., Collart M.A., (2019) Switch from translation initiation to elongation needs Not4 and Not5 collaboration. bioRxiv, 850859
  13. Roch M., Lelong-Alborini E., Panasenko O.O., Sierra R., Renzoni A., Kelley W.L. (2019) PBP2A: a temperature sensitive enzyme requiring extracellular folding factors, PrsA and HtrA1, for β-lactam resistance in Staphylococcus aureus MRSA, Communications Biology, 2, 417
  14. Panasenko O.O., Somasekharan S.P., Villanyi Z., Zagatti M., Bezrukov F., Rashpa R., Cornut J, Iqbal J., Longis M., Carl S.H., Peña C., Panse V.G., Collart M.A. (2019) Co-translational assembly of proteasome subunits in NOT1-containing assemblysomes, Nature Structural & Molecular Biology, 26, 110
  15. Collart M.A., Panasenko O.O. (2017) The Ccr4-Not complex: Architecture and structural insights, Subcellular Biochemistry, chapter in a book “Macromolecular Protein Complexes”, 83, 349
  16. Gupta I., Villanyi Z., Kassem S., Hughes C., Panasenko O.O., Steinmetz L., Collart M.A. (2016), Translational capacity of a cell is determined during transcription elongation via the Ccr4-Not complex, Cell Reports, 15, 1782
  17. Villanyi Z., Ribaud V., Kassem S., Panasenko O.O., Pahi Z., Boros I., Collart M.A. (2014), Not5 subunit of the Ccr4-Not complex connects transcription and translation, PLoS Genet., 10, e1004569
  18. Panasenko O.O. (2014) The role of E3 ligase, Not4, in cotranslational quality control, Front.Genet, 5, 141
  19. Panasenko O.O. (2014) Identification of ubiquitinated proteins, Material and Methods, 4, 827.
  20. Halter D., Collart M.A., Panasenko O.O. (2014) The Not4 E3 ligase and Caf1/Ccr4 deadenylase play distinct roles in protein quality control, PLoS ONE, 9, e86218.
  21. Collart M.A., Panasenko O.O., Nikolaev S. (2013) The Not3/5 subunit of the Ccr4-Not complex: a central regulator of gene expression that integrates signals between the cytoplasm and the nucleus in eukaryotic cells, Cellular Signaling, 25, 743.
  22. Panasenko O.O. (2012) Co-immunoprecipitation in Yeast, Bio-protocol, 2 (16), e250.
  23. Collart M.A., Panasenko O.O. (2012) The Ccr4-Not4 complex, Gene, 492, 42.
  24. Panasenko O.O., Collart M.A. (2012) Presence of Not5 and ubiquitinated Rps7A in polysome fractions depends upon the Not4 E3 ligase, Mol. Microbiol.,83, 640.
  25. Panasenko O.O. (2012) Ribosome Fractionation in Yeast, Bio-protocol, 2 (16), e251.
  26. Panasenko O.O., Collart M.A. (2011) Not4 E3 ligase contributes to proteasome assembly and functional integrity in part through Ecm29, Mol Cell Biol, 31, 1610.
  27. Azzouz N., Panasenko O.O., Colau G., Collart M.A. (2009) The CCR4-NOT complex physically and functionally connects TRAMP and the nuclear exosome, PLoS ONE, 4, e6760.
  28. Panasenko O.O., Fabrice P.A.D., Collart M.A. (2009) Ribosome association and stability of the nascent polypeptide associated complex is dependent upon its own ubiquitination, Genetics, 181, 447.
  29. Azzouz N., Panasenko O.O., Deluen, C., Hsieh, J., Theiler, G., Collart M.A. (2009) Specific roles for the CCR4-NOT complex subunits in expression of the genome, RNA, 15, 377.
  30. Panasenko O., Landrieux E., Feuermann M., Finka A., Paquet N., Collart M.A. (2006) The yeast CCR4-NOT complex controls ubiquitination of the nascent associated polypeptide complex (NAC), J Biol Chem., 281, 31389.
  31. Chernik I.S., Panasenko O.O., Li Y., Marston S.B., Gusev N.B. (2004) pH-induced changes of the structure of small heat shock protein with molecular mass 25/27 kDa (HspB1), BBRC, 324, 1199.
  32. Panasenko O.O, Metzler D., Bekhite M.M., Wartenberg M. (2004) A phosphomimic mutant of the small heat shock protein hsp25 induces a Ca2+-insensitive contraction in chemically skinned smooth muscle, European Journal of Cell Biology, 83, 44.
  33. Panasenko O.O., Kim, M.V., Gusev N.B. (2003) Structure and properties of small heat shock protein (sHSP), Progress of Biol. Chemistry, 43, 59.
  34. Panasenko O.O., Kim, M.V., Marston S.B., Gusev N.B. (2003) Interaction of the small heat shock protein with molecular weight 25 kDa (HSP25) with actin, European Journal of Biochem., 270, 892
  35. Panasenko O.O., Seit-Nebi A., Bukach O.V., Marston S.B., Gusev N.B. (2002) Structure and properties of avian small heat shock protein (sHSP) with apparent molecular weight 25 kDa, Biochim Biophys Acta - Proteins and Proteomics, 1601, 64.
  36. Bukach O.V., Seit Nebi A. S, Panasenko O.O., Kim M.V., Gusev N.B. (2002) Isolation of tissue and recombinant small heat shock protein with molecular weight 25 kDa (HSP25) from avian smooth muscles, Problems of Biol., Med. and Pharmaceutical Chemistry, 1, 50
  37. Panasenko O.O., Gusev N.B. (2001) Mutual effects of alpha-actinin, calponin and filamin on actin binding, Biochim Biophys Acta - Protein Structure and Molecular Enzymology, 1544, 393.
  38. Panasenko O.O., Gusev N.B. (2000) Simultaneous interaction of actin with alpha-actinin and calponin, IUBMB Life, 49, 277.
  39. Panasenko O.M., Panasenko O.O., Briviba K., Sies H. (1997) Hypochlorite destroys carotenoids in low density lipoproteins decreasing their resistance to peroxidative modification, Biochemistry (Mosc), 62, 1140.

Team