A unique tRNA recognition mechanism of Caenorhabditis elegans mitochondrial EF-Tu2.

Abstract:

:Nematode mitochondria expresses two types of extremely truncated tRNAs that are specifically recognized by two distinct elongation factor Tu (EF-Tu) species named EF-Tu1 and EF-Tu2. This is unlike the canonical EF-Tu molecule that participates in the standard protein biosynthesis systems, which basically recognizes all elongator tRNAs. EF-Tu2 specifically recognizes Ser-tRNA(Ser) that lacks a D arm but has a short T arm. Our previous study led us to speculate the lack of the D arm may be essential for the tRNA recognition of EF-Tu2. However, here, we showed that the EF-Tu2 can bind to D arm-bearing Ser-tRNAs, in which the D-T arm interaction was weakened by the mutations. The ethylnitrosourea-modification interference assay showed that EF-Tu2 is unique, in that it interacts with the phosphate groups on the T stem on the side that is opposite to where canonical EF-Tu binds. The hydrolysis protection assay using several EF-Tu2 mutants then strongly suggests that seven C-terminal amino acid residues of EF-Tu2 are essential for its aminoacyl-tRNA-binding activity. Our results indicate that the formation of the nematode mitochondrial (mt) EF-Tu2/GTP/aminoacyl-tRNA ternary complex is probably supported by a unique interaction between the C-terminal extension of EF-Tu2 and the tRNA.

journal_name

Nucleic Acids Res

journal_title

Nucleic acids research

authors

Suematsu T,Sato A,Sakurai M,Watanabe K,Ohtsuki T

doi

10.1093/nar/gki784

keywords:

subject

Has Abstract

pub_date

2005-08-19 00:00:00

pages

4683-91

issue

15

eissn

0305-1048

issn

1362-4962

pii

33/15/4683

journal_volume

33

pub_type

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