scholarly journals Structure of Human Mitochondrial Translation Initiation Factor 3 Bound to the Small Ribosomal Subunit

iScience ◽  
2019 ◽  
Vol 12 ◽  
pp. 76-86 ◽  
Author(s):  
Ravi K. Koripella ◽  
Manjuli R. Sharma ◽  
Md. Emdadul Haque ◽  
Paul Risteff ◽  
Linda L. Spremulli ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Ribosomal Subunit ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Mitochondrial Translation ◽  
Small Ribosomal Subunit ◽  
Translation Initiation Factor 3

Mitochondrial translation initiation factor 3 polymorphism and Parkinson's disease

2010 ◽  
Vol 486 (3) ◽  
pp. 228-230 ◽  
Author(s):  
Bahareh Behrouz ◽  
Carles Vilariño-Güell ◽  
Michael G. Heckman ◽  
Alexandra I. Soto-Ortolaza ◽  
Jan O. Aasly ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Translation Initiation ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Mitochondrial Translation ◽  
Translation Initiation Factor 3

scholarly journals rRNA Suppressor of a Eukaryotic Translation Initiation Factor 5B/Initiation Factor 2 Mutant Reveals a Binding Site for Translational GTPases on the Small Ribosomal Subunit

2008 ◽  
Vol 29 (3) ◽  
pp. 808-821 ◽  
Author(s):  
Byung-Sik Shin ◽  
Joo-Ran Kim ◽  
Michael G. Acker ◽  
Kathryn N. Maher ◽  
Jon R. Lorsch ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Ribosomal Subunit ◽  
The Body ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Small Ribosomal Subunit ◽  
Eukaryotic Translation Initiation Factor ◽  
Eukaryotic Translation ◽  
Initiation Factor 2 ◽  
Eukaryotic Translation Initiation

ABSTRACT The translational GTPases promote initiation, elongation, and termination of protein synthesis by interacting with the ribosome. Mutations that impair GTP hydrolysis by eukaryotic translation initiation factor 5B/initiation factor 2 (eIF5B/IF2) impair yeast cell growth due to failure to dissociate from the ribosome following subunit joining. A mutation in helix h5 of the 18S rRNA in the 40S ribosomal subunit and intragenic mutations in domain II of eIF5B suppress the toxic effects associated with expression of the eIF5B-H480I GTPase-deficient mutant in yeast by lowering the ribosome binding affinity of eIF5B. Hydroxyl radical mapping experiments reveal that the domain II suppressors interface with the body of the 40S subunit in the vicinity of helix h5. As the helix h5 mutation also impairs elongation factor function, the rRNA and eIF5B suppressor mutations provide in vivo evidence supporting a functionally important docking of domain II of the translational GTPases on the body of the small ribosomal subunit.

scholarly journals Yeast Mitochondrial Translation Initiation Factor 3 Interacts with Pet111p to Promote COX2 mRNA Translation

2020 ◽  
Vol 21 (10) ◽  
pp. 3414
Author(s):  
Ivan Chicherin ◽  
Sergey Levitskii ◽  
Maria V. Baleva ◽  
Igor A. Krasheninnikov ◽  
Maxim V. Patrushev ◽  
...  
Keyword(s):  
Translation Initiation ◽  
Mitochondrial Protein ◽  
Mrna Translation ◽  
Translation Initiation Factor ◽  
Yeast Cells ◽  
Initiation Factor ◽  
Specific Factor ◽  
Mitochondrial Translation ◽  
Respiratory Chain Complexes ◽  
Translation Initiation Factor 3

Mitochondrial genomes code for several core components of respiratory chain complexes. Thus, mitochondrial translation is of great importance for the organelle as well as for the whole cell. In yeast, mitochondrial translation initiation factor 3, Aim23p, is not essential for the organellar protein synthesis; however, its absence leads to a significant quantitative imbalance of the mitochondrial translation products. This fact points to a possible specific action of Aim23p on the biosynthesis of some mitochondrial protein species. In this work, we examined such peculiar effects of Aim23p in relation to yeast mitochondrial COX2 mRNA translation. We show that Aim23p is indispensable to this process. According to our data, this is mediated by Aimp23p interaction with the known specific factor of the COX2 mRNA translation, Pet111p. If there is no Aim23p in the yeast cells, an increased amount of Pet111p ensures proper COX2 mRNA translation. Our results demonstrate the additional non-canonical function of initiation factor 3 in yeast mitochondrial translation.

scholarly journals Possible Involvement of a Mitochondrial Translation Initiation Factor 3 Variant Causing Decreased mRNA Levels in Parkinson's Disease

2010 ◽  
Vol 2010 ◽  
pp. 1-5 ◽  
Author(s):  
Anna Anvret ◽  
Caroline Ran ◽  
Marie Westerlund ◽  
Ann-Christin Thelander ◽  
Olof Sydow ◽  
...  
Keyword(s):  
Parkinson’S Disease ◽  
Parkinson's Disease ◽  
Translation Initiation ◽  
Mitochondrial Function ◽  
Case Control ◽  
Translation Initiation Factor ◽  
Initiation Factor ◽  
Mitochondrial Translation ◽  
Control Material ◽  
Translation Initiation Factor 3

Genes important for mitochondrial function have been implicated in Parkinson's disease (PD). Mitochondrial translation initiation factor 3 (MTIF3) is a nuclear encoded protein required for the initiation of complex formation on mitochondrial ribosomes. Dysfunction of MTIF3 may impair mitochondrial function and dopamine neurons appear to be particularly vulnerable to oxidative stress, which may relate to their degeneration in PD. An association was recently reported between the synonymous rs7669(C>T) in MTIF3 and PD in a German case-control material. We investigated rs7669 in a Swedish Parkinson case-control material. The study revealed no significant association of the individual genotypes or alleles with PD. When comparing the combined TT/CT-genotypes versus the CC-genotype, we observed a significant association (P=.0473) with PD. We also demonstrated that the TT-genotype causes a significant decrease in MTIF3 mRNA expression compared to the CC-genotype (P=.0163). Our findings support the hypothesis that MTIF3 may be involved in the etiology of PD.

Sign in / Sign up

Export Citation Format

Share Document