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Specific binding of tRNAMet to 23S rRNA of Escherichia coli.
Author(s) -
J E Dahlberg,
Chris Kintner,
Elsebet Lund
Publication year - 1978
Publication title -
proceedings of the national academy of sciences
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.75.3.1071
Subject(s) - 23s ribosomal rna , ribosome , ribosomal rna , transfer rna , escherichia coli , sequence (biology) , biology , nucleotide , p site , ribosomal protein , rna , genetics , microbiology and biotechnology , biochemistry , gene
tRNAMetf binds to 23S rRNA of Escherichia coli, forming a complex with a melting temperature of 75 degrees (in 0.6 M NaCl). The regions within the RNAs that bind to each other have been isolated and their nucleotide sequences have been determined. The interacting region in tRNAMetf is 17 nucleotides long, extending from G5 in the acceptor stem to D21 (D = 5.6-dihydrouridine) in the D loop. The sequence in 23S rRNA is complementary to that sequence except for an extra Up in the middle and allowing a Gp.D base pair. We propose that association of these two sequences may play a role in initiation of protein synthesis by tRNAMetf. In addition, part of this sequence in 23S rRNA may also stabilize tRNA binding to the ribosome during elongation of nascent polypeptides.

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