An unusual pattern of protein expression and localization of yeast alanyl-tRNA synthetase isoforms.

Abstract:

:Previous studies have shown that in Saccharomyces cerevisiae the mitochondrial and cytoplasmic forms of alanyl-tRNA synthetase are encoded by a single nuclear gene, ALA1, through alternative use of in-frame successive ACG triplets and a downstream AUG triplet. Here we show that despite the obvious participation of the non-AUG-initiated leader peptide in mitochondrial localization, the leader peptide per se cannot target a cytoplasmic passenger protein into mitochondria under normal conditions. Functional mapping further shows that an efficient targeting signal is composed of the leader peptide and an 18-residue sequence downstream of Met1. Consistent to this observation, overexpression of the cytoplasmic form enables it to overcome the compartmental barrier and function in the mitochondria as well, but deletion of as few as eight amino acid residues from its amino-terminus eliminates such a potential. Thus, the sequence upstream of the first in-frame AUG initiator not only carries an unusual initiation site, but also contributes to a novel pattern of protein expression and localization.

journal_name

Mol Microbiol

journal_title

Molecular microbiology

authors

Huang HY,Tang HL,Chao HY,Yeh LS,Wang CC

doi

10.1111/j.1365-2958.2006.05083.x

subject

Has Abstract

pub_date

2006-04-01 00:00:00

pages

189-98

issue

1

eissn

0950-382X

issn

1365-2958

pii

MMI5083

journal_volume

60

pub_type

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