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PMID: 8052601 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Human cytoplasmic isoleucyl-tRNA synthetase: selective divergence of the anticodon-binding domain and acquisition of a new structural unit.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 16 ·1994-08-02 ·Pages 7435-9

Shiba K, Suzuki N, Shigesada K, Namba Y, Schimmel P, Noda T

Abstract

We show here that the class I human cytoplasmic isoleucyl-tRNA synthetase is an exceptionally large polypeptide (1266 aa) which, unlike its homologues in lower eukaryotes and prokaryotes, has a third domain of two repeats of an approximately 90-aa sequence appended to its C-terminal end. While extracts of Escherichia coli do not aminoacrylate mammalian tRNA with isoleucine, expression of the cloned human gene in E. coli results in charging of the mammalian tRNA substrate. The appended third domain is dispensable for detection of this aminoacylation activity and may be needed for assembly of a multisynthetase complex in mammalian cells. Alignment of the sequences of the remaining two domains shared by isoleucyl-tRNA synthetases from E. coli to human reveals a much greater selective pressure on the domain needed for tRNA acceptor helix interactions and catalysis than on the domain needed for interactions with the anticodon. This result may have implications for the historical development of an operational RNA code for amino acids.

MeSH Terms
Amino Acid Sequence Cell Compartmentation Cloning, Molecular Cytoplasm/enzymology DNA Transposable Elements Escherichia coli/genetics Humans Isoleucine-tRNA Ligase/genetics,metabolism Molecular Sequence Data RNA, Transfer, Leu/metabolism Recombinant Proteins/metabolism Repetitive Sequences, Nucleic Acid Sequence Analysis, DNA Sequence Homology, Amino Acid Species Specificity Structure-Activity Relationship
Chemicals
DNA Transposable Elements RNA, Transfer, Leu Recombinant Proteins Isoleucine-tRNA Ligase
Authors & Affiliations
6 authors, click to expand affiliations / ORCID
Shiba K
Department of Cell Biology, Cancer Institute, Tokyo, Japan.
Suzuki N
Shigesada K
Namba Y
Schimmel P
Noda T
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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.91.16.7435
Published
1994-08-02
Pages
7435-9
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC44415
Subset
IM
Grants
NIGMS NIH HHS · GM15539 · United States
Databases
GENBANK
D28473
External Links
PubMed source DOI: 10.1073/pnas.91.16.7435 PMC Full Text View journal details
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