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The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

Author(s): Leibovitch M, Bublak D, Hanic-Joyce PJ, Tillmann B, Flinner N, Amsel D, Scharf KD, Mirus O, Joyce PB, Schleiff E

Biochem J. 2013 Aug 01;453(3):401-12 Authors: Leibovitch M, Bublak D, Hanic-Joyce PJ, Tillmann B, Flinner N, Amsel D, Scharf KD, Mirus O, Joyce PB, Schleiff E

Article GUID: 23713568
In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.

Author(s): Leibovitch M, Hanic-Joyce PJ, Joyce PBM

Biochim Biophys Acta Proteins Proteom. 2018 Apr;1866(4):527-540 Authors: Leibovitch M, Hanic-Joyce PJ, Joyce PBM

Article GUID: 29454993
Analysis of the pathogenic I326T variant of human tRNA nucleotidyltransferase reveals reduced catalytic activity and thermal stability in vitro linked to a conformational change.

Author(s): Leibovitch M, Reid NE, Victoria J, Hanic-Joyce PJ, Joyce PBM

Biochim Biophys Acta Proteins Proteom. 2019 Jun;1867(6):616-626 Authors: Leibovitch M, Reid NE, Victoria J, Hanic-Joyce PJ, Joyce PBM

Article GUID: 30959222
Title:The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.
Authors:Leibovitch M,  Bublak D,  Hanic-Joyce PJ,  Tillmann B,  Flinner N,  Amsel D,  Scharf KD,  Mirus O,  Joyce PB,  Schleiff E
Link:https://www.ncbi.nlm.nih.gov/pubmed/23713568?dopt=Abstract
DOI:10.1042/BJ20121577
Category:Biochem J
PMID:23713568
Dept Affiliation: GENOMICS
1 Department of Chemistry and Biochemistry and Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke St. W., Montréal, Québec, Canada H4B 1R6.

Description:

The folding capacity of the mature domain of the dual-targeted plant tRNA nucleotidyltransferase influences organelle selection.

Biochem J. 2013 Aug 01;453(3):401-12

Authors: Leibovitch M, Bublak D, Hanic-Joyce PJ, Tillmann B, Flinner N, Amsel D, Scharf KD, Mirus O, Joyce PB, Schleiff E

Abstract

tRNA-NTs (tRNA nucleotidyltransferases) are required for the maturation or repair of tRNAs by ensuring that they have an intact cytidine-cytidine-adenosine sequence at their 3'-termini. Therefore this enzymatic activity is found in all cellular compartments, namely the nucleus, cytoplasm, plastids and mitochondria, in which tRNA synthesis or translation occurs. A single gene codes for tRNA-NT in plants, suggesting a complex targeting mechanism. Consistent with this, distinct signals have been proposed for plastidic, mitochondrial and nuclear targeting. Our previous research has shown that in addition to N-terminal targeting information, the mature domain of the protein itself modifies targeting to mitochondria and plastids. This suggests the existence of an as yet unknown determinate for the distribution of dual-targeted proteins between these two organelles. In the present study, we explore the enzymatic and physicochemical properties of tRNA-NT variants to correlate the properties of the enzyme with the intracellular distribution of the protein. We show that alteration of tRNA-NT stability influences its intracellular distribution due to variations in organelle import capacities. Hence the fate of the protein is determined not only by the transit peptide sequence, but also by the physicochemical properties of the mature protein.

PMID: 23713568 [PubMed - indexed for MEDLINE]