Biochemical and Structural Studies of A-to-I Editing by tRNA:A34 Deaminases at the Wobble Position of Transfer RNA†,‡

Biochemistry ◽  
2005 ◽  
Vol 44 (36) ◽  
pp. 12057-12065 ◽  
Author(s):  
Youssef Elias ◽  
Raven H. Huang
Keyword(s):  
Transfer Rna ◽  
Structural Studies ◽  
Wobble Position

Thiolation of uridine carbon-2 restricts the motional dynamics of the transfer RNA wobble position nucleoside

1992 ◽  
Vol 114 (7) ◽  
pp. 2652-2656 ◽  
Author(s):  
Paul F. Agris ◽  
Hanna Sierzputowska-Gracz ◽  
Wanda Smith ◽  
A. Malkiewicz ◽  
Elzbieta Sochacka ◽  
...  
Keyword(s):  
Transfer Rna ◽  
Wobble Position ◽  
Motional Dynamics

Structural Studies on Transfer RNA: Preliminary Crystallographic Analysis

Science ◽  
1969 ◽  
Vol 166 (3912) ◽  
pp. 1530-1532 ◽  
Author(s):  
M. Labanauskas ◽  
P. G. Connors ◽  
J. D. Young ◽  
R. M. Bock ◽  
J. W. Anderegg ◽  
...  
Keyword(s):  
Transfer Rna ◽  
Crystallographic Analysis ◽  
Structural Studies

scholarly journals Absolute requirement for polyamines for growth of Escherichia coli mutants (mnmE/G) defective in modification of the wobble anticodon of transfer-RNA

2019 ◽  
Vol 366 (10) ◽  
Author(s):  
Christopher Keller ◽  
Manas Chattopadhyay ◽  
Herbert Tabor
Keyword(s):  
Escherichia Coli ◽  
Growth Rate ◽  
Protein Biosynthesis ◽  
Transfer Rna ◽  
Coli Strain ◽  
E Coli ◽  
Wobble Position ◽  
Inhibition Of Growth ◽  
Absolute Requirement

Abstract The genes mnmE and mnmG are responsible for the modification of uridine 34, ‘the wobble position’ of many aminoacyl-tRNAs. Deletion of these genes affects the strength of the codon-anticodon interactions of the aminoacyl-tRNAs with the mRNAs and the ribosomes. However, deletion of these genes does not usually have a significant effect on the growth rate of the standard Escherichia coli strains. In contrast, we have found that if the host E. coli strain is deficient in the synthesis of polyamines, deletion of the mnmE or mnmG gene results in complete inhibition of growth unless the medium contains polyamines. The finding of an absolute requirement for polyamines in our current work will be significant in studies on polyamine function, in studies on the function of the mnmE/G genes, and in studies on the role of aminoacyl-tRNAs in protein biosynthesis.

scholarly journals 7-Methylguanosine Modifications in Transfer RNA (tRNA)

2018 ◽  
Vol 19 (12) ◽  
pp. 4080 ◽  
Author(s):  
Chie Tomikawa
Keyword(s):  
Reaction Mechanism ◽  
Thermophilic Bacteria ◽  
Variable Region ◽  
Transfer Rna ◽  
Modified Nucleosides ◽  
Structural Studies ◽  
Trna Modifications ◽  
The Past ◽  
Methyl Transfer ◽  
Trna Structure

More than 90 different modified nucleosides have been identified in tRNA. Among the tRNA modifications, the 7-methylguanosine (m7G) modification is found widely in eubacteria, eukaryotes, and a few archaea. In most cases, the m7G modification occurs at position 46 in the variable region and is a product of tRNA (m7G46) methyltransferase. The m7G46 modification forms a tertiary base pair with C13-G22, and stabilizes the tRNA structure. A reaction mechanism for eubacterial tRNA m7G methyltransferase has been proposed based on the results of biochemical, bioinformatic, and structural studies. However, an experimentally determined mechanism of methyl-transfer remains to be ascertained. The physiological functions of m7G46 in tRNA have started to be determined over the past decade. For example, tRNA m7G46 or tRNA (m7G46) methyltransferase controls the amount of other tRNA modifications in thermophilic bacteria, contributes to the pathogenic infectivity, and is also associated with several diseases. In this review, information of tRNA m7G modifications and tRNA m7G methyltransferases is summarized and the differences in reaction mechanism between tRNA m7G methyltransferase and rRNA or mRNA m7G methylation enzyme are discussed.

Structural Studies on Transfer RNA: Crystallization of Formylmethionine and Leucine Transfer RNA's

Science ◽  
1969 ◽  
Vol 166 (3912) ◽  
pp. 1527-1528 ◽  
Author(s):  
J. D. Young ◽  
R. M. Bock ◽  
S. Nishimura ◽  
H. Ishikura ◽  
Y. Yamada ◽  
...  
Keyword(s):  
Transfer Rna ◽  
Structural Studies

ChemInform Abstract: Chemistry and Structure of Modified Uridines in the Anticodon, Wobble Position of Transfer RNA Are Determined by Thiolation

ChemInform ◽  
1988 ◽  
Vol 19 (10) ◽  
Author(s):  
H. SIERZPUTOWSKA-GRACZ ◽  
E. SOCHACKA ◽  
A. MALKIEWICZ ◽  
K. KUO ◽  
C. W. GEHRKE ◽  
...  
Keyword(s):  
Transfer Rna ◽  
Wobble Position

Chemistry and structure of modified uridines in the anticodon, wobble position of transfer RNA are determined by thiolation

1987 ◽  
Vol 109 (23) ◽  
pp. 7171-7177 ◽  
Author(s):  
Hanna Sierzputowska-Gracz ◽  
Elzbieta Sochacka ◽  
Andrzej Malkiewicz ◽  
Kenneth Kuo ◽  
Charles W. Gehrke ◽  
...  
Keyword(s):  
Transfer Rna ◽  
Wobble Position
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