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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:In vitro studies of disease-linked variants of human tRNA nucleotidyltransferase reveal decreased thermal stability and altered catalytic activity.
Authors:Leibovitch M,  Hanic-Joyce PJ,  Joyce PBM
Link:https://www.ncbi.nlm.nih.gov/pubmed/29454993?dopt=Abstract
Category:Biochim Biophys Acta Proteins Proteom
PMID:29454993
Dept Affiliation: CHEMBIOCHEM
1 Department of Chemistry and Biochemistry and Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke St. W., Montréal H4B 1R6, Québec, Canada.
2 Department of Chemistry and Biochemistry and Centre for Structural and Functional Genomics, Concordia University, 7141 Sherbrooke St. W., Montréal H4B 1R6, Québec, Canada. Electronic address: paul.joyce@concordia.ca.

Description:

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

Biochim Biophys Acta Proteins Proteom. 2018 Apr;1866(4):527-540

Authors: Leibovitch M, Hanic-Joyce PJ, Joyce PBM

Abstract

Mutations in the human TRNT1 gene encoding tRNA nucleotidyltransferase (tRNA-NT), an essential enzyme responsible for addition of the CCA (cytidine-cytidine-adenosine) sequence to the 3'-termini of tRNAs, have been linked to disease phenotypes including congenital sideroblastic anemia with B-cell immunodeficiency, periodic fevers and developmental delay (SIFD) or retinitis pigmentosa with erythrocyte microcytosis. The effects of these disease-linked mutations on the structure and function of tRNA-NT have not been explored. Here we use biochemical and biophysical approaches to study how five SIFD-linked amino acid substitutions (T154I, M158V, L166S, R190I and I223T), residing in the N-terminal head and neck domains of the enzyme, affect the structure and activity of human tRNA-NT in vitro. Our data suggest that the SIFD phenotype is linked to poor stability of the T154I and L166S variant proteins, and to a combination of reduced stability and altered catalytic efficiency in the M158?V, R190I and I223T variants.

PMID: 29454993 [PubMed - indexed for MEDLINE]