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Mycobacterium tuberculosis Rv2118c codes for a single-component homotetrameric m1A58 tRNA methyltransferase.

U Varshney1, V Ramesh, A Madabushi

  • 1Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.

Nucleic Acids Research
|February 13, 2004
PubMed
Summary
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Mycobacterium tuberculosis Rv2118p is an S-adenosyl-l-methionine-dependent methyltransferase that modifies tRNA at A58. This enzyme, a homotetramer, is essential for mycobacterial growth and a potential drug target.

Area of Science:

  • Molecular Biology
  • Biochemistry
  • Microbiology

Background:

  • Modified nucleosides in tRNAs are vital for bacterial growth and virulence.
  • N1-methylation of adenosine 58 (m1A58) in initiator tRNA is essential for Saccharomyces cerevisiae viability.
  • While absent in most bacteria, m1A58 is present in mycobacterial tRNAs.

Purpose of the Study:

  • To clone, overexpress, purify, and biochemically characterize the Rv2118c gene-encoded protein (Rv2118p) from Mycobacterium tuberculosis.
  • To investigate the enzymatic activity and properties of Rv2118p as an m1A58 tRNA methyltransferase.
  • To explore the potential of Rv2118p as a drug target for controlling mycobacterial growth.

Main Methods:

  • Cloning and overexpression of the Rv2118c gene.

Related Experiment Videos

  • Purification of the recombinant Rv2118p protein.
  • Biochemical assays, including activity assays, modified base analysis, and primer extension experiments using reverse transcriptase.

    • Main Results:

    • Rv2118p is an S-adenosyl-l-methionine-dependent methyltransferase responsible for m1A58 modification in tRNAs.
    • The enzyme functions both in vivo and in vitro, efficiently methylating endogenous Escherichia coli initiator tRNA when expressed in E. coli.
    • Unlike its eukaryotic counterpart, the mycobacterial enzyme functions as a homotetramer and is unaffected by rT modification at position 54.

    Conclusions:

    • Rv2118p is a distinct mycobacterial m1A58 tRNA methyltransferase with unique biochemical properties compared to its eukaryotic homolog.
    • The enzyme's essential role in mycobacterial biology suggests its potential as a novel drug target for tuberculosis treatment.
    • Understanding Rv2118p's function provides insights into tRNA modification pathways in pathogenic bacteria.