RSM22, mtYsxC and PNKD-like proteins are required for mitochondrial translation in Trypanosoma brucei

0479262 - BC 2018 RIV NL eng J - Journal Article
Týč, Jiří - Novotná, L. - Peña-Diaz, Priscila - Maslov, D. A. - Lukeš, Julius
RSM22, mtYsxC and PNKD-like proteins are required for mitochondrial translation in Trypanosoma brucei.
Mitochondrion. Roč. 34, MAY (2017), s. 67-74. ISSN 1567-7249. E-ISSN 1872-8278
R&D Projects: GA ČR GA15-21974S
Institutional support: RVO:60077344
Keywords : PNKD * YsxC * YihA * mitochondrial ribosome * LSU * SSU
OECD category: Genetics and heredity (medical genetics to be 3)
Impact factor: 3.226, year: 2017

Mitochondrial ribosomes evolved from prokaryotic ribosomes, with which they therefore share more common features than with their counterparts in the cytosol. Yet, mitochondrial ribosomes are highly diverse in structure and composition, having undergone considerable changes, including reduction of their RNA component and varying degree of acquisition of novel proteins in various phylogenetic lineages. Here, we present functional analysis of three putative mitochondrial ribosome-associated proteins (RSM22, mtYsxC and PNKD-like) in Trypanosoma brucei, originally identified by database mining. While in other systems the homologs of RSM22 are known as components of mitochondria ribosomes, YsxC was linked with ribosomes only in bacteria. The PNKD-like protein shows similarity to a human protein, the defects of which cause PNKD (paroxysmal nonkinesigenic dyskinesia). Here we show that all three proteins are important for the growth of T. brucei. They play an important function in mitochondrial translation, as their ablation by RNAi rapidly and severely affected the de novo synthesis of mitochondrial proteins. Moreover, following the RNAi-mediated depletion of RSM22, structure of the small subunit of mitochondrial ribosome becomes severely compromised, suggesting a role of RSM22 in ribosomal assembly and/or stability. (C) 2017 Elsevier B.V. and Mitochondria Research Society. All rights reserved.
Permanent Link: http://hdl.handle.net/11104/0275259