Chathuri Pathirage

ORCID: 0000-0003-1527-0882
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About
Contact & Profiles
Research Areas
  • HIV Research and Treatment
  • RNA and protein synthesis mechanisms
  • RNA modifications and cancer
  • RNA Research and Splicing
  • Cytomegalovirus and herpesvirus research
  • Bacteriophages and microbial interactions
  • HIV/AIDS drug development and treatment

The Ohio State University
2021-2025

The average eukaryotic transfer ribonucleic acid (tRNA) contains 13 post-transcriptional modifications; however, their functional impact is largely unknown. Our understanding of the complex tRNA aminoacylation machinery in metazoans also remains limited. Herein, using a series high-resolution cryo-electron microscopy (cryo-EM) structures, we provide mechanistic basis for recognition and fully modified cellular tRNALys3 by human lysyl-tRNA synthetase (h-LysRS). anticodon loop modifications...

10.1093/nar/gkaf114 article EN cc-by Nucleic Acids Research 2025-02-06

Interactions between lysyl-tRNA synthetase (LysRS) and HIV-1 Gag facilitate selective packaging of the reverse transcription primer, tRNA

10.3390/v14071556 article EN cc-by Viruses 2022-07-16

Abstract Background During HIV-1 maturation, Gag and Gag-Pol polyproteins are proteolytically cleaved the capsid protein polymerizes to form honeycomb lattice. integrase (IN) binds viral genomic RNA (gRNA) impairment of IN-gRNA binding leads mis-localization nucleocapsid (NC)-condensed ribonucleoprotein complex outside core. IN NC were previously demonstrated bind gRNA in an orthogonal manner virio; however, effect alone or simultaneous both proteins on structure is not yet well understood....

10.1186/s12977-021-00582-0 article EN cc-by Retrovirology 2021-11-22

ABSTRACT The average eukaryotic tRNA contains 13 posttranscriptional modifications; however, their functional impact is largely unknown. Our understanding of the complex aminoacylation machinery in metazoans also remains limited. Herein, using a series high-resolution cryo-electron microscopy (cryo-EM) structures, we provide mechanistic basis for recognition and fully-modified cellular Lys3 by human lysyl-tRNA synthetase (h-LysRS). anticodon loop modifications S34 (mcm 5 s 2 U) R37 (ms t 6...

10.1101/2024.12.07.627298 preprint EN cc-by-nc-nd bioRxiv (Cold Spring Harbor Laboratory) 2024-12-08
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