| Full text | |
| Author(s): |
Santos, Barbara
[1]
;
Zeng, Rui
[2]
;
Jorge, Sasa F.
[1]
;
Ferreira-Junior, Jose Ribamar
[3]
;
Barrientos, Antoni
[2]
;
Barros, Mario H.
[1]
Total Authors: 6
|
| Affiliation: | [1] Univ Sao Paulo, Dept Microbiol, Sao Paulo - Brazil
[2] Univ Miami, Miller Sch Med, Dept Neurol, Miami, FL 33136 - USA
[3] Univ Sao Paulo, Escola Artes Ciencias & Humanidades, Sao Paulo - Brazil
Total Affiliations: 3
|
| Document type: | Journal article |
| Source: | YEAST; NOV 2021. |
| Web of Science Citations: | 0 |
| Abstract | |
In Saccharomyces cerevisiae, mitoribosomes are composed of a 54S large subunit (mtLSU) and a 37S small subunit (mtSSU). The two subunits altogether contain 73 mitoribosome proteins (MRPs) and two ribosomal RNAs (rRNAs). Although mitoribosomes preserve some similarities with their bacterial counterparts, they have significantly diverged by acquiring new proteins, protein extensions, and new RNA segments, adapting the mitoribosome to the synthesis of highly hydrophobic membrane proteins. In this study, we investigated the functional relevance of mitochondria-specific protein extensions at the C-terminus (C) or N-terminus (N) present in 19 proteins of the mtLSU. The studied mitochondria-specific extensions consist of long tails and loops extending from globular domains that mainly interact with mitochondria-specific proteins and 21S rRNA moieties extensions. The expression of variants devoid of extensions in uL4 (C), uL5 (N), uL13 (N), uL13 (C), uL16 (C), bL17 (N), bL17 (C), bL21 (24), uL22 (N), uL23 (N), uL23 (C), uL24 (C), bL27 (C), bL28 (N), bL28 (C), uL29 (N), uL29 (C), uL30 (C), bL31 (C), and bL32 (C) did not rescue the mitochondrial protein synthesis capacities and respiratory growth of the respective null mutants. On the contrary, the truncated form of the mitoribosome exit tunnel protein uL24 (N) yields a partially functional mitoribosome. Also, the removal of mitochondria-specific sequences from uL1 (N), uL3 (N), uL16 (N), bL9 (N), bL19 (C), uL29 (C), and bL31 (N) did not affect the mitoribosome function and respiratory growth. The collection of mutants described here provides new means to study and evaluate defective assembly modules in the mitoribosome biogenesis process. (AU) | |
| FAPESP's process: | 13/07937-8 - Redoxome - Redox Processes in Biomedicine |
| Grantee: | Ohara Augusto |
| Support Opportunities: | Research Grants - Research, Innovation and Dissemination Centers - RIDC |
| FAPESP's process: | 20/05812-7 - Regulation events for mitoribossome biogenesis and respiratory complexes assembly |
| Grantee: | Mario Henrique de Barros |
| Support Opportunities: | Regular Research Grants |
| FAPESP's process: | 18/03253-0 - Study of the formation of the mitoribosome exit tunnel and impact in mitochondria translation |
| Grantee: | Barbara Santos de Oliveira |
| Support Opportunities: | Scholarships in Brazil - Scientific Initiation |
| FAPESP's process: | 17/23921-5 - Study of mitochondrial translation factors |
| Grantee: | Mario Henrique de Barros |
| Support Opportunities: | Regular Research Grants |