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PMID: 1103137 Published · ppublish English Journal Article

Site of aminoacylation of tRNAs from Escherichia coli with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 72 ·No. 8 ·1975-08-00 ·Pages 3049-53

Sprinzl M, Cramer F

Abstract

A method is presented by which the site of primary attachment of the amino acids with respect to the 2'- or 3'-hydroxyl group of the terminal adenosine of E. coli tRNAs can be determined. It is found that the aminoacyl-tRNA synthetases (EC 6.1.1.-) with specificity for Arg, Asn, Ile, Leu, Met, Phe, Thr, Trp, and Val attach the amino acid to the 2'-position; those with specificity for Gly, His, Lys, and Ser attach the amino acid to the 3'-position; and that Tyr and Cys can be enzymatically attached to both the 2'- and 3'-positions. Together with previous experiments on yeast aminoacyl-tRNA synthetases, it is now shown that the specificity for one particular hydroxyl group is preserved during the evolution from prokaryotic to eukaryotic systems.

MeSH Terms
Adenosine/analysis Amino Acids Amino Acyl-tRNA Synthetases/metabolism Animals Base Sequence Escherichia coli/enzymology Liver/enzymology RNA, Transfer/analysis Rats Saccharomyces cerevisiae/enzymology Species Specificity Transfer RNA Aminoacylation
Chemicals
Amino Acids RNA, Transfer Amino Acyl-tRNA Synthetases Adenosine
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Sprinzl M
Cramer F
References (19)
19 references, click to expand
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.72.8.3049
Published
1975-08-00
Pages
3049-53
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC432916
Subset
IM
External Links
PubMed source DOI: 10.1073/pnas.72.8.3049 PMC Full Text View journal details
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