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PMID: 331261 Published · ppublish English Journal Article Research Support, U.S. Gov't, Non-P.H.S. Research Support, U.S. Gov't, P.H.S.

Structural organization of complexes of transfer RNAs with aminoacyl transfer RNA synthetases.

Nucleic acids research ·Vol. 4 ·No. 5 ·1977-00-00 ·Pages 1649-65

Rich A, Schimmel PR

Abstract

A variety of experimental data on synthetase-tRNA interactions are examined. Although these data previously had no direct explanation when viewed only in terms of the tRNA cloverleaf diagram, they can be rationalized according to a simple proposal that takes account of the three dimensional structure of tRNA. It is proposed that a major part of the binding site for most or all synthetases is along and around the diagonal side of the tRNA structure, which contains the acceptor stem, dihydrouridine stem, and anticodon. This side of the tRNA molecule contains structural features likely to be common for all tRNAs. Depending on the system, an enzyme may span a small part or all of the region of this side of the molecule. Interactions with other parts of the structure may also occur in a manner that varies from complex to complex. These interactions may be determined, in part, by the angle at which the diagonal side of the flat tRNA molecule is inserted onto the surface of the synthetase.

MeSH Terms
Amino Acyl-tRNA Synthetases/metabolism Anticodon Base Sequence Binding Sites Nucleic Acid Conformation Phenylalanine Protein Binding RNA, Transfer RNA, Viral Saccharomyces cerevisiae
Chemicals
Anticodon RNA, Viral Phenylalanine RNA, Transfer Amino Acyl-tRNA Synthetases
Authors & Affiliations
2 authors, click to expand affiliations / ORCID
Rich A
Schimmel P R
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52 references, click to expand
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/4.5.1649
Published
1977-00-00
Pages
1649-65
Language
English
Region
England
NLM ID
0411011
PMCID
PMC343779
Subset
IM
External Links
PubMed source DOI: 10.1093/nar/4.5.1649 PMC Full Text View journal details
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