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PMID: 9636067 Published · ppublish English Comparative Study Journal Article Research Support, U.S. Gov't, P.H.S.

Strong selective pressure to use G:U to mark an RNA acceptor stem for alanine.

Biochemistry ·Vol. 37 ·No. 25 ·1998-06-23 ·Pages 9193-202

Chihade JW, Hayashibara K, Shiba K, Schimmel P

Abstract

The identity of alanine tRNAs is dependent on a G:U base pair at the 3:70 position of the acceptor helix. This system of molecular recognition is widely distributed from bacteria to human-cell cytoplasm. In contrast, some mitochondrial alanine acceptor helices are markedly different and contain nucleotides known to block aminoacylation by a nonmitochondrial enzyme. Thus, acceptor helix recognition may differ in these systems and may not depend on G:U. Here we report an example of a Caenorhabditis elegans mitochondrial system where the G:U pair is preserved but where proximal nucleotides known to block charging by a nonmitochondrial enzyme are also present. We show that, as expected, the mitochondrial substrate is not charged by the bacterial enzyme. In contrast, the cloned mitochondrial enzyme charged both mitochondrial and bacterial microhelices. Strikingly, charging of each required the G:U pair. Thus, G:U recognition persists even with an acceptor helix context that inactivates nonmitochondrial systems. The results suggest strong selective pressure to use G:U in a variety of contexts to mark an acceptor stem for alanine. Separate experiments also demonstrate that, at least for the mitochondrial enzyme, helix instability or irregularity is not important for recognition of G:U.

MeSH Terms
Acylation Alanine-tRNA Ligase/chemistry,genetics Amino Acid Sequence Animals Base Composition Base Sequence Caenorhabditis elegans/enzymology,genetics Cloning, Molecular Escherichia coli/enzymology,genetics Guanine/chemistry Humans Mitochondria/enzymology Molecular Sequence Data Mutagenesis, Site-Directed Protein Conformation Sequence Homology, Amino Acid Substrate Specificity/genetics Uracil/chemistry
Chemicals
Uracil Guanine Alanine-tRNA Ligase
Authors & Affiliations
4 authors, click to expand affiliations / ORCID
Chihade J W
Department of Biology, Massachusetts Institute of Technology, Cambridge 02139, USA.
Hayashibara K
Shiba K
Schimmel P
Article Info
Journal
Biochemistry
Abbr.
Biochemistry
ISSN
0006-2960
Published
1998-06-23
Pages
9193-202
Language
English
Region
United States
NLM ID
0370623
Subset
IM
Grants
NIGMS NIH HHS · GM15539 · United States
NIGMS NIH HHS · GM23562 · United States
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