Experience

Korro Bio, Inc.

• United States
• Biotechnology Research
• 1 - 100 Employee

• Principal Scientist

  • Mar 2022 - Present



Penn State University

• United States
• Higher Education
• 700 & Above Employee

• Associate Research Professor

  • Oct 2017 - Mar 2022

  Developed the purification procedures for all 9 yeast RNase P and 10 RNase MRP proteins. Those proteins were purified from strain superproducent in native conditions. Pop1 protein and heterodimer complexes of Pop6/Pop7 and Rpp1/Pop5 proteins were purified without any tags. In collaboration with Professor Raymund Wellinger’s laboratory (Universite de Sherbrooke, Canada) we discovered, that Pop1/Pop6/Pop7 binding is specific and involves an RNA domain highly similar to a protein-binding domain in… Show more Developed the purification procedures for all 9 yeast RNase P and 10 RNase MRP proteins. Those proteins were purified from strain superproducent in native conditions. Pop1 protein and heterodimer complexes of Pop6/Pop7 and Rpp1/Pop5 proteins were purified without any tags. In collaboration with Professor Raymund Wellinger’s laboratory (Universite de Sherbrooke, Canada) we discovered, that Pop1/Pop6/Pop7 binding is specific and involves an RNA domain highly similar to a protein-binding domain in the RNAs of RNase P/MRP. The results also show that Pop1/Pop6/Pop7 function to maintain the essential components Est1 and Est2 on the RNA in vivo. •Developed a robust approach to the in vitro reconstitution of Saccharomyces cerevisiae RNase P RNPs and used it to analyze the interplay and roles of RNase P components. •In collaboration with Professor Susan Hafenstein’s laboratory (Pennsylvania State University) the cryo-EM structure of RNAse MRP was solved.

• Research Associate

  • Nov 2012 - Oct 2017

• Postdoctoral Fellow

  • Jun 2006 - Oct 2012

  Conduct biochemical and structural studies of RNase MRP (yeast) including: determination of binding sites of RNA for specific proteins; preparation of a small fragment of RNA - those that are specifically bound with the proteins; and crystallization of proteins and protein-RNA complexes. Have supervisory responsibilities for 1 graduate student and 3 undergraduate students. Developed purification procedures for 8 from 10th of yeast RNase MRP proteins: Rpp1/Pop5 heterodimer, Pop8, Pop4, SNM1… Show more Conduct biochemical and structural studies of RNase MRP (yeast) including: determination of binding sites of RNA for specific proteins; preparation of a small fragment of RNA - those that are specifically bound with the proteins; and crystallization of proteins and protein-RNA complexes. Have supervisory responsibilities for 1 graduate student and 3 undergraduate students. Developed purification procedures for 8 from 10th of yeast RNase MRP proteins: Rpp1/Pop5 heterodimer, Pop8, Pop4, SNM1 and Pop3. Pop6/Pop7 heterodimer was purified in native conditions and without tags. Found specific binding site of Pop6/Pop7 protein complex and Rpp1/Pop5 protein complex at MRP RNA. Developed and purified fragment of MRP RNA which specific binds with Pop6/Pop7 heterodimer. Complex of Pop6/Pop7 heterodimer with that RNA fragment was crystallized; selenometionine substitute of the proteins was obtained. Introducing mutation in Pop6 protein allowed us to improve the crystals' quality and structure of the complex was solved. SNM1 protein was crystallized.



University of Alabama at Birmingham

• Higher Education
• 700 & Above Employee

• Postdoctoral Fellow

  • Apr 2005 - May 2006

  Continued the project work under Dr. Dmitry Vassylyev at the University of Alabama that was started in 2003 in Japan and wrote several papers that were published in several scientific journals. Continued the project work under Dr. Dmitry Vassylyev at the University of Alabama that was started in 2003 in Japan and wrote several papers that were published in several scientific journals.



RIKEN

• Japan
• Research Services
• 700 & Above Employee

• Contract Researcher

  • Oct 2003 - Mar 2005

  Conducted structural studies of transcription regulation (multi-subunit RNA polymerases as complexes with transcription factors and nucleic acids) aimed at understanding mechanism of regulation and inhibition transcription in prokaryotic organisms. • Developed procedure for purification transcription factors GreA, Gfh1 (Thermus thermophilus), GreB, YacL (E. coli), helicases SrmB, DbpA (E. coli). Gfh1, GreB, RfaH, DksA proteins and complex RfaH with specific fragment of DNA were crystallized.… Show more Conducted structural studies of transcription regulation (multi-subunit RNA polymerases as complexes with transcription factors and nucleic acids) aimed at understanding mechanism of regulation and inhibition transcription in prokaryotic organisms. • Developed procedure for purification transcription factors GreA, Gfh1 (Thermus thermophilus), GreB, YacL (E. coli), helicases SrmB, DbpA (E. coli). Gfh1, GreB, RfaH, DksA proteins and complex RfaH with specific fragment of DNA were crystallized. Selenometionine substitute of GreB, RfaH, Gfh1 proteins were obtained and structure of Gfh1, DksA and RfaH were solved. Crystals of RNA polymerase holoenzyme (T. thermophilus) with antibiotics rifapentin, rifabutin, tagetin, streptolydigin and DNA aptomer were obtained. Show less Conducted structural studies of transcription regulation (multi-subunit RNA polymerases as complexes with transcription factors and nucleic acids) aimed at understanding mechanism of regulation and inhibition transcription in prokaryotic organisms. • Developed procedure for purification transcription factors GreA, Gfh1 (Thermus thermophilus), GreB, YacL (E. coli), helicases SrmB, DbpA (E. coli). Gfh1, GreB, RfaH, DksA proteins and complex RfaH with specific fragment of DNA were crystallized.… Show more Conducted structural studies of transcription regulation (multi-subunit RNA polymerases as complexes with transcription factors and nucleic acids) aimed at understanding mechanism of regulation and inhibition transcription in prokaryotic organisms. • Developed procedure for purification transcription factors GreA, Gfh1 (Thermus thermophilus), GreB, YacL (E. coli), helicases SrmB, DbpA (E. coli). Gfh1, GreB, RfaH, DksA proteins and complex RfaH with specific fragment of DNA were crystallized. Selenometionine substitute of GreB, RfaH, Gfh1 proteins were obtained and structure of Gfh1, DksA and RfaH were solved. Crystals of RNA polymerase holoenzyme (T. thermophilus) with antibiotics rifapentin, rifabutin, tagetin, streptolydigin and DNA aptomer were obtained. Show less



Institute of Protein Research

• Researcher

  • 2002 - 2003