98%
921
2 minutes
20
Unlabelled: possesses four initiator tRNA (i-tRNA) genes, three of which are present together as and the fourth one as . In B, all four genes ( and ) encode i-tRNA, in which the G at position 46 is modified to mG46 by TrmB (mG methyltransferase). However, in K, because of a single-nucleotide polymorphism, encodes a variant, i-tRNA, having an A in place of mG46. We generated strains to explore the importance of this polymorphism in i-tRNAs. The strains were sustained either on ( of K origin encoding i-tRNA) or its derivative (encoding i-tRNA) in single (chromosomal) or plasmid-borne copies. We show that the strains sustained on i-tRNA have a growth fitness advantage over those sustained on i-tRNA. The growth fitness advantages are more pronounced for the strains sustained on i-tRNA in nutrient-rich media than in nutrient-poor media. The growth fitness of the strains correlates well with the relative stabilities of the i-tRNAs . Furthermore, the atomistic molecular dynamics simulations support the higher stability of i-tRNA than that of i-tRNA. The stability of i-tRNA remains unaffected upon the deletion of TrmB. These studies highlight how and alleles might influence the growth fitness of under certain nutrient-limiting conditions.
Importance: harbors four initiator tRNA (i-tRNA) genes: three of these at and the fourth one at loci. In B, all four genes encode i-tRNA. In K, because of a single-nucleotide polymorphism, metY encodes a variant, i-tRNA, having an A in place of G at position 46 of i-tRNA sequence in metY. We show that G46 confers stability to i-tRNA. The strains sustained on i-tRNA have a growth fitness advantage over those sustained on i-tRNA. Strains harboring (B mimic) or (K mimic) show that while in the nutrient-rich media, the K mimic is outcompeted rapidly; in the nutrient-poor medium, the K mimic is outcompeted less rapidly.
Download full-text PDF |
Source |
---|---|
http://www.ncbi.nlm.nih.gov/pmc/articles/PMC11411947 | PMC |
http://dx.doi.org/10.1128/jb.00251-24 | DOI Listing |
J Bacteriol
September 2024
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
Unlabelled: possesses four initiator tRNA (i-tRNA) genes, three of which are present together as and the fourth one as . In B, all four genes ( and ) encode i-tRNA, in which the G at position 46 is modified to mG46 by TrmB (mG methyltransferase). However, in K, because of a single-nucleotide polymorphism, encodes a variant, i-tRNA, having an A in place of mG46.
View Article and Find Full Text PDFNucleic Acids Res
November 2022
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore 560012, India.
Initiation factor 3 (IF3) regulates the fidelity of bacterial translation initiation by debarring the use of non-canonical start codons or non-initiator tRNAs and prevents premature docking of the 50S ribosomal subunit to the 30S pre-initiation complex (PIC). The C-terminal domain (CTD) of IF3 can carry out most of the known functions of IF3 and sustain Escherichia coli growth. However, the roles of the N-terminal domain (NTD) have remained unclear.
View Article and Find Full Text PDFMol Microbiol
February 2022
Department of Microbiology and Cell Biology, Indian Institute of Science, Bangalore, India.
The anticodon stem of initiator tRNA (i-tRNA) possesses the characteristic three consecutive GC base pairs (G29:C41, G30:C40, and G31:C39 abbreviated as GC/GC/GC or 3GC pairs) crucial to commencing translation. To understand the importance of this highly conserved element, we isolated two fast-growing suppressors of Escherichia coli sustained solely on an unconventional i-tRNA (i-tRNA ) having cg/GC/cg sequence instead of the conventional GC/GC/GC. Both suppressors have the common mutation of V93A in initiation factor 3 (IF3), and additional mutations of either V32L (Sup-1) or H76L (Sup-2) in small subunit ribosomal protein 12 (uS12).
View Article and Find Full Text PDFJ Mol Evol
September 2004
Ocean Research Institute, University of Tokyo, 1-15-1 Minamidai, Nakano-ku, Tokyo 164-8639, Japan.
Genomic size of animal mitochondrial DNA is usually minimized over time. Thus, when regional duplications occur, they are followed by a rapid elimination of redundant material. In contrast to this general view, we report here long-sustained tRNA pseudogenes in the mitochondrial genome (mitogenome) of teleost fishes of the family Scaridae (parrotfishes).
View Article and Find Full Text PDFJ Biol Chem
August 1994
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139.
We present evidence that zinc bound near the C terminus of a long tRNA synthetase polypeptide, and at a location far in the sequence from the catalytic domain, is needed to sustain cell growth and is, therefore, essential for enzyme function. Several class I and class II tRNA synthetases contain bound zinc, including the 939-amino acid class I Escherichia coli isoleucyl-tRNA synthetase, which has two zinc atoms coordinated to cysteine sulfhydryls. The functional significance of these bound zinc atoms has been unclear.
View Article and Find Full Text PDF