scholarly journals Switching a conflicted bacterial DTD-tRNA code is essential for the emergence of mitochondria

2022 ◽  
Vol 8 (2) ◽  
Author(s):  
Jotin Gogoi ◽  
Akshay Bhatnagar ◽  
Kezia. J. Ann ◽  
Sambhavi Pottabathini ◽  
Raghvendra Singh ◽  
...  
Keyword(s):  
Discriminator Base

Optimization of DTD-tRNA code and mito-tRNA(Gly) discriminator base is important for emergence of mitochondria.

scholarly journals Fluorescence probing of T box antiterminator RNA: Insights into riboswitch discernment of the tRNA discriminator base

2009 ◽  
Vol 389 (4) ◽  
pp. 616-621 ◽  
Author(s):  
John A. Means ◽  
Crystal M. Simson ◽  
Shu Zhou ◽  
Aaron A. Rachford ◽  
Jeffrey J. Rack ◽  
...  
Keyword(s):  
T Box ◽  
Fluorescence Probing ◽  
Discriminator Base

scholarly journals The discriminator base influences tRNA structure at the end of the acceptor stem and possibly its interaction with proteins.

1993 ◽  
Vol 90 (15) ◽  
pp. 7149-7152 ◽  
Author(s):  
C. P. Lee ◽  
N. Mandal ◽  
M. R. Dyson ◽  
U. L. RajBhandary
Keyword(s):  
Acceptor Stem ◽  
Trna Structure ◽  
Discriminator Base

scholarly journals Development of Assay Systems for Amber Codon Decoding at the Steps of Initiation and Elongation in Mycobacteria

2018 ◽  
Vol 200 (22) ◽  
Author(s):  
Ashwin Govindan ◽  
Sandeep Miryala ◽  
Sanjay Mondal ◽  
Umesh Varshney
Keyword(s):  
Protein Synthesis ◽  
Genetic Analysis ◽  
Structure Function ◽  
Translation Initiation ◽  
Base Pair ◽  
Content Type ◽  
Gram Positive Bacteria ◽  
Base Position ◽  
Discriminator Base

ABSTRACTGenetic analysis of the mechanism of protein synthesis in Gram-positive bacteria has remained largely unexplored because of the unavailability of appropriatein vivoassay systems. We developed chloramphenicol acetyltransferase (CAT)-basedin vivoreporter systems to study translation initiation and elongation inMycobacterium smegmatis. The CAT reporters utilize specific decoding of amber codons by mutant initiator tRNA (i-tRNA,metU) molecules containing a CUA anticodon (metUCUA). The assay systems allow structure-function analyses of tRNAs without interfering with the cellular protein synthesis and function with or without the expression of heterologous GlnRS fromEscherichia coli. We show that despite their naturally occurring slow-growth phenotypes, the step of i-tRNA formylation is vital in translation initiation in mycobacteria and that formylation-deficient i-tRNA mutants (metUCUA/A1,metUCUA/G72, andmetUCUA/G72G73) with a Watson-Crick base pair at the 1·72 position participate in elongation. In the absence of heterologous GlnRS expression, the mutant tRNAs are predominantly aminoacylated (glutamylated) by nondiscriminating GluRS. Acid urea gels show complete transamidation of the glutamylatedmetUCUA/G72G73tRNA to its glutaminylated form (by GatCAB) inM. smegmatis. In contrast, the glutamylatedmetUCUA/G72tRNA did not show a detectable level of transamidation. Interestingly, themetUCUA/A1mutant showed an intermediate activity of transamidation and accumulated in both glutamylated and glutaminylated forms. These observations suggest important roles for the discriminator base position and/or a weak Watson-Crick base pair at 1·72 forin vivorecognition of the glutamylated tRNAs byM. smegmatisGatCAB.IMPORTANCEGenetic analysis of the translational apparatus in Gram-positive bacteria has remained largely unexplored because of the unavailability of appropriatein vivoassay systems. We developed chloramphenicol acetyltransferase (CAT)-based reporters which utilize specific decoding of amber codons by mutant tRNAs at the steps of initiation and/or elongation to allow structure-function analysis of the translational machinery. We show that formylation of the initiator tRNA (i-tRNA) is crucial even for slow-growing bacteria and that i-tRNA mutants with a CUA anticodon are aminoacylated by nondiscriminating GluRS. The discriminator base position, and/or a weak Watson-Crick base pair at the top of the acceptor stem, provides important determinants for transamidation of the i-tRNA-attached Glu to Gln by the mycobacterial GatCAB.

scholarly journals NMR analysis of tRNA acceptor stem microhelices: discriminator base change affects tRNA conformation at the 3' end.

1994 ◽  
Vol 91 (24) ◽  
pp. 11467-11471 ◽  
Author(s):  
E. V. Puglisi ◽  
J. D. Puglisi ◽  
J. R. Williamson ◽  
U. L. RajBhandary
Keyword(s):  
Base Change ◽  
Nmr Analysis ◽  
Acceptor Stem ◽  
Discriminator Base ◽  
Trna Acceptor

scholarly journals Identification of Discriminator Base Atomic Groups That Modulate the Alanine Aminoacylation Reaction

1999 ◽  
Vol 274 (52) ◽  
pp. 37093-37096 ◽  
Author(s):  
Abbey E. Fischer ◽  
Penny J. Beuning ◽  
Karin Musier-Forsyth
Keyword(s):  
Discriminator Base

Discriminator base of tRNAAsp is involved in amino acid acceptor activity

1989 ◽  
Vol 163 (3) ◽  
pp. 1534-1538 ◽  
Author(s):  
Tsunemi Hasegawa ◽  
Hyouta Himeno ◽  
Hisayuki Ishikura ◽  
Mikio Shimizu
Keyword(s):  
Amino Acid ◽  
Acceptor Activity ◽  
Discriminator Base ◽  
Amino Acid Acceptor

scholarly journals The anticodon and discriminator base are major determinants of cysteine tRNA identity in vivo.

1992 ◽  
Vol 267 (11) ◽  
pp. 7221-7223 ◽  
Author(s):  
L Pallanck ◽  
S Li ◽  
L.H. Schulman
Keyword(s):  
Discriminator Base

scholarly journals Discrimination of amino acid by anticodon and discriminator base.

1979 ◽  
Vol 55 (8) ◽  
pp. 387-392 ◽  
Author(s):  
Mikio SHIMIZU
Keyword(s):  
Amino Acid ◽  
Discriminator Base

scholarly journals The exchange of the discriminator base A73 for G is alone sufficient to convert human tRNA(Leu) into a serine-acceptor in vitro.

1994 ◽  
Vol 13 (13) ◽  
pp. 3166-3169 ◽  
Author(s):  
K. Breitschopf ◽  
H.J. Gross
Keyword(s):  
Discriminator Base

scholarly journals Recognition by Tryptophanyl-tRNA Synthetases of Discriminator Base on tRNATrpfrom Three Biological Domains

2002 ◽  
Vol 277 (16) ◽  
pp. 14343-14349 ◽  
Author(s):  
Qing Guo ◽  
Qingguo Gong ◽  
Ka-Lok Tong ◽  
Bente Vestergaard ◽  
Annie Costa ◽  
...  
Keyword(s):  
Trna Synthetases ◽  
Discriminator Base
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