ASSOCIATION OF TRNA(GLN) ACCEPTOR IDENTITY WITH PHOSPHATE-SUGAR BACKBONE INTERACTIONS OBSERVED IN THE CRYSTAL-STRUCTURE OF THE ESCHERICHIA-COLI GLUTAMINYL-TRANSFER-RNA SYNTHETASE-TRNA(GLN) COMPLEX

Authors
MCCLAIN WH SCHNEIDER J GABRIEL K
Citation
Wh. Mcclain et al., ASSOCIATION OF TRNA(GLN) ACCEPTOR IDENTITY WITH PHOSPHATE-SUGAR BACKBONE INTERACTIONS OBSERVED IN THE CRYSTAL-STRUCTURE OF THE ESCHERICHIA-COLI GLUTAMINYL-TRANSFER-RNA SYNTHETASE-TRNA(GLN) COMPLEX, Biochimie, 75(12), 1993, pp. 1125-1136
Citations number
50
Categorie Soggetti
Biology
Journal title
Biochimie → ACNP
ISSN journal
03009084
Volume
75
Issue
12
Year of publication
1993
Pages
1125 - 1136
Database
ISI
SICI code
0300-9084(1993)75:12<1125:AOTAIW>2.0.ZU;2-K
Abstract
We isolated several mutants with nucleotide substitutions in alanine t RNA (tRNA(A1a)) that resulted in glutamine tRNA (tRNA(G1n)) acceptor i dentity in Escherichia coli. These substitutions were in three regions of tRNA structure not previously associated with tRNA(G1n) acceptor i dentity. Only the phosphate-sugar backbone moieties of these nucleotid es interact with the enzyme in the pre viously determined X-ray crysta l structure of the complex between tRNA(G1n) and glutaminyl-tRNA synth etase. We conclude that these sequence-dependent phosphate-sugar backb one interactions contribute to tRNA(G1n) identity, and argue that the interactions help communicate enzyme recognition of the anticodon to t he acceptor end of the tRNA and the catalytic center of the enzyme.