22 results on '"Kamenski, A. A."'
Search Results
2. Mitochondrial Protein SLIRP Affects Biosynthesis of Cytochrome c Oxidase Subunits in HEK293T Cells
- Author
-
Mariia V. Baleva, Uliana Piunova, Ivan Chicherin, Ruslan Vasilev, Sergey Levitskii, and Piotr Kamenski
- Subjects
mitochondria ,translation ,translation regulation ,Biology (General) ,QH301-705.5 ,Chemistry ,QD1-999 - Abstract
Mitochondria carry out various vital roles in eukaryotic cells, including ATP energy synthesis, the regulation of apoptosis, Fe-S cluster formation, and the metabolism of fatty acids, amino acids, and nucleotides. Throughout evolution, mitochondria lost most of their ancestor’s genome but kept the replication, transcription, and translation machinery. Protein biosynthesis in mitochondria is specialized in the production of highly hydrophobic proteins encoded by mitochondria. These proteins are components of oxidative phosphorylation chain complexes. The coordination of protein synthesis must be precise to ensure the correct assembly of nuclear-encoded subunits for these complexes. However, the regulatory mechanisms of mitochondrial translation in human cells are not yet fully understood. In this study, we examined the contribution of the SLIRP protein in regulating protein biosynthesis in mitochondria. Using a click-chemistry approach, we discovered that deletion of the SLIRP gene disturbs mitochondrial translation, leading to the dysfunction of complexes I and IV, but it has no significant effect on complexes III and V. We have shown that this protein interacts only with the small subunit of the mitochondrial ribosome, which may indicate its involvement in the regulation of the mitochondrial translation initiation stage.
- Published
- 2023
- Full Text
- View/download PDF
3. Yeast Translational Activator Mss51p and Human ZMYND17 – Two Proteins with a Common Origin, but Different Functions
- Author
-
Baleva, Maria V., Piunova, Uliyana E., Chicherin, Ivan V., Krasavina, Darya G., Levitskii, Sergey A., and Kamenski, Piotr A.
- Published
- 2021
- Full Text
- View/download PDF
4. Pentatricopeptide Protein PTCD2 Regulates COIII Translation in Mitochondria of the HeLa Cell Line
- Author
-
Maria V. Baleva, Ivan Chicherin, Uliana Piunova, Viktor Zgoda, Maxim V. Patrushev, Sergey Levitskii, and Piotr Kamenski
- Subjects
mitochondria ,translation ,translation regulation ,Biology (General) ,QH301-705.5 ,Chemistry ,QD1-999 - Abstract
Protein biosynthesis in mitochondria is tightly coupled with assembly of inner membrane complexes and therefore must be coordinated with cytosolic translation of the mRNAs corresponding to the subunits which are encoded in the nucleus. Molecular mechanisms underlying the regulation of mitochondrial translation remain unclear despite recent advances in structural biology. Until now, only one translational regulator of protein biosynthesis in mammalian mitochondria is known—protein TACO1, which regulates translation of COI mRNA. Here we describe the function of pentatricopeptide-containing protein PTCD2 as a translational regulator of another mitochondrially encoded subunit of cytochrome c oxidase—COIII in the HeLa cell line. Deletion of the PTCD2 gene leads to significant decrease in COIII translation efficiency and impairment in CIV activity. Additionally, we show that PTCD2 protein is partially co-sedimentates with associated mitochondrial ribosome and associates with mitochondrial ribosome proteins in pull-down assays. These data allow concluding that PTCD2 is a specific translational regulator of COIII which attracts the mRNA to the mitochondrial ribosome.
- Published
- 2022
- Full Text
- View/download PDF
5. Protein Biosynthesis in Mitochondria: Past Simple, Present Perfect, Future Indefinite
- Author
-
Levitskii, S. A., Baleva, M. V., Chicherin, I. V., Krasheninnikov, I. A., and Kamenski, P. A.
- Published
- 2020
- Full Text
- View/download PDF
6. Functional Diversity of Mitochondrial Peptidyl-tRNA Hydrolase ICT1 in Human Cells
- Author
-
I.V. Chicherin, S.V. Dukhalin, R.A. Khannanov, M.V. Baleva, S.A. Levitskii, M.V. Patrushev, P.V. Sergiev, and P. Kamenski
- Subjects
mitochondria ,translation ,termination ,regulation ,apoptosis ,cell cycle ,Biology (General) ,QH301-705.5 - Abstract
Mitochondria are energy producing organelles of the eukaryotic cell, involved in the synthesis of key metabolites, calcium homeostasis and apoptosis. Protein biosynthesis in these organelles is a relic of its endosymbiotic origin. While mitochondrial translational factors have homologues among prokaryotes, they possess a number of unique traits. Remarkably as many as four mammalian mitochondrial proteins possess a clear similarity with translation termination factors. The review focuses on the ICT1, which combines several functions. It is a non-canonical termination factor for protein biosynthesis, a rescue factor for stalled mitochondrial ribosomes, a structural protein and a regulator of proliferation, cell cycle, and apoptosis. Such a diversity of roles demonstrates the high functionality of mitochondrial translation associated proteins and their relationship with numerous processes occurring in a living cell.
- Published
- 2021
- Full Text
- View/download PDF
7. Mitochondrial Protein SLIRP Affects Biosynthesis of Cytochrome c Oxidase Subunits in HEK293T Cells.
- Author
-
Baleva, Mariia V., Piunova, Uliana, Chicherin, Ivan, Vasilev, Ruslan, Levitskii, Sergey, and Kamenski, Piotr
- Subjects
CYTOCHROME oxidase ,MITOCHONDRIAL proteins ,BIOSYNTHESIS ,PROTEIN synthesis ,EUKARYOTIC cells ,OXIDATIVE phosphorylation ,GENETIC translation - Abstract
Mitochondria carry out various vital roles in eukaryotic cells, including ATP energy synthesis, the regulation of apoptosis, Fe-S cluster formation, and the metabolism of fatty acids, amino acids, and nucleotides. Throughout evolution, mitochondria lost most of their ancestor's genome but kept the replication, transcription, and translation machinery. Protein biosynthesis in mitochondria is specialized in the production of highly hydrophobic proteins encoded by mitochondria. These proteins are components of oxidative phosphorylation chain complexes. The coordination of protein synthesis must be precise to ensure the correct assembly of nuclear-encoded subunits for these complexes. However, the regulatory mechanisms of mitochondrial translation in human cells are not yet fully understood. In this study, we examined the contribution of the SLIRP protein in regulating protein biosynthesis in mitochondria. Using a click-chemistry approach, we discovered that deletion of the SLIRP gene disturbs mitochondrial translation, leading to the dysfunction of complexes I and IV, but it has no significant effect on complexes III and V. We have shown that this protein interacts only with the small subunit of the mitochondrial ribosome, which may indicate its involvement in the regulation of the mitochondrial translation initiation stage. [ABSTRACT FROM AUTHOR]
- Published
- 2024
- Full Text
- View/download PDF
8. Activation of Yeast Mitochondrial Translation: Who Is in Charge?
- Author
-
Derbikova, K. S., Levitsky, S. A., Chicherin, I. V., Vinogradova, E. N., and Kamenski, P. A.
- Published
- 2018
- Full Text
- View/download PDF
9. 60S dynamic state of bacterial ribosome is fixed by yeast mitochondrial initiation factor 3
- Author
-
Sergey Levitskii, Ksenia Derbikova, Maria V. Baleva, Anton Kuzmenko, Andrey V. Golovin, Ivan Chicherin, Igor A. Krasheninnikov, and Piotr Kamenski
- Subjects
Ribosome ,Initiation factor 3 ,Subunit dissociation ,Translation ,Medicine ,Biology (General) ,QH301-705.5 - Abstract
The processes of association and dissociation of ribosomal subunits are of great importance for the protein biosynthesis. The mechanistic details of these processes, however, are not well known. In bacteria, upon translation termination, the ribosome dissociates into subunits which is necessary for its further involvement into new initiation step. The dissociated state of the ribosome is maintained by initiation factor 3 (IF3) which binds to free small subunits and prevents their premature association with large subunits. In this work, we have exchanged IF3 in Escherichia coli cells by its ortholog from Saccharomyces cerevisiae mitochondria (Aim23p) and showed that yeast protein cannot functionally substitute the bacterial one and is even slightly toxic for bacterial cells. Our in vitro experiments have demonstrated that Aim23p does not split E. coli ribosomes into subunits. Instead, it fixes a state of ribosomes characterized by sedimentation coefficient about 60S which is not a stable structure but rather reflects a shift of dynamic equilibrium between associated and dissociated states of the ribosome. Mitochondria-specific terminal extensions of Aim23p are necessary for “60S state” formation, and molecular modeling results point out that these extensions might stabilize the position of the protein on the bacterial ribosome.
- Published
- 2018
- Full Text
- View/download PDF
10. Yeast Mitochondrial Translation Initiation Factor 3 Interacts with Pet111p to Promote COX2 mRNA Translation
- Author
-
Ivan Chicherin, Sergey Levitskii, Maria V. Baleva, Igor A. Krasheninnikov, Maxim V. Patrushev, and Piotr Kamenski
- Subjects
mitochondria ,translation ,initiation factor ,translational activator ,Biology (General) ,QH301-705.5 ,Chemistry ,QD1-999 - Abstract
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.
- Published
- 2020
- Full Text
- View/download PDF
11. Mitochondrial Targeting of RNA and Mitochondrial Translation
- Author
-
Tarassov, Ivan, Chicherin, Ivan, Tonin, Yann, Smirnov, Alexandre, Kamenski, Petr, Entelis, Nina, and Duchêne, Anne-Marie, editor
- Published
- 2013
- Full Text
- View/download PDF
12. Biological and Evolutionary Significance of Terminal Extensions of Mitochondrial Translation Initiation Factor 3
- Author
-
Ksenia Derbikova, Anton Kuzmenko, Sergey Levitskii, Maria Klimontova, Ivan Chicherin, Maria V. Baleva, Igor A. Krasheninnikov, and Piotr Kamenski
- Subjects
mitochondria ,translation ,initiation ,initiation factor ,terminal extension ,Biology (General) ,QH301-705.5 ,Chemistry ,QD1-999 - Abstract
Protein biosynthesis in mitochondria is organized in a bacterial manner. However, during evolution, mitochondrial translation mechanisms underwent many organelle-specific changes. In particular, almost all mitochondrial translation factors, being orthologous to bacterial proteins, are characterized by some unique elements of primary or secondary structure. In the case of the organellar initiation factor 3 (IF3), these elements are several dozen amino acids long N- and C-terminal extensions. This study focused on the terminal extensions of baker’s yeast mitochondrial IF3, Aim23p. By in vivo deletion and complementation analysis, we show that at least one extension is necessary for Aim23p function. At the same time, human mitochondrial IF3 is fully functional in yeast mitochondria even without both terminal extensions. While Escherichia coli IF3 itself is poorly active in yeast mitochondria, adding Aim23p terminal extensions makes the resulting chimeric protein as functional as the cognate factor. Our results show that the terminal extensions of IF3 have evolved as the “adaptors„ that accommodate the translation factor of bacterial origin to the evolutionary changed protein biosynthesis system in mitochondria.
- Published
- 2018
- Full Text
- View/download PDF
13. Pentatricopeptide Protein PTCD2 Regulates COIII Translation in Mitochondria of the HeLa Cell Line.
- Author
-
Baleva, Maria V., Chicherin, Ivan, Piunova, Uliana, Zgoda, Viktor, Patrushev, Maxim V., Levitskii, Sergey, and Kamenski, Piotr
- Subjects
RIBOSOMES ,HELA cells ,CYTOCHROME oxidase ,CELL lines ,GENETIC translation ,MITOCHONDRIAL proteins ,MITOCHONDRIA - Abstract
Protein biosynthesis in mitochondria is tightly coupled with assembly of inner membrane complexes and therefore must be coordinated with cytosolic translation of the mRNAs corresponding to the subunits which are encoded in the nucleus. Molecular mechanisms underlying the regulation of mitochondrial translation remain unclear despite recent advances in structural biology. Until now, only one translational regulator of protein biosynthesis in mammalian mitochondria is known—protein TACO1, which regulates translation of COI mRNA. Here we describe the function of pentatricopeptide-containing protein PTCD2 as a translational regulator of another mitochondrially encoded subunit of cytochrome c oxidase—COIII in the HeLa cell line. Deletion of the PTCD2 gene leads to significant decrease in COIII translation efficiency and impairment in CIV activity. Additionally, we show that PTCD2 protein is partially co-sedimentates with associated mitochondrial ribosome and associates with mitochondrial ribosome proteins in pull-down assays. These data allow concluding that PTCD2 is a specific translational regulator of COIII which attracts the mRNA to the mitochondrial ribosome. [ABSTRACT FROM AUTHOR]
- Published
- 2022
- Full Text
- View/download PDF
14. Protein biosynthesis in mitochondria
- Author
-
Kuzmenko, A. V., Levitskii, S. A., Vinogradova, E. N., Atkinson, G. C., Hauryliuk, V., Zenkin, N., and Kamenski, P. A.
- Published
- 2013
- Full Text
- View/download PDF
15. Initiation Factor 3 is Dispensable For Mitochondrial Translation in Cultured Human Cells
- Author
-
I. V. Chicherin, Maria V. Baleva, Piotr Kamenski, S. A. Levitskii, E. B. Dashinimaev, and Igor A. Krasheninnikov
- Subjects
Translation ,Messenger RNA ,Multidisciplinary ,ATP synthase ,Molecular biology ,Mitochondrial translation ,lcsh:R ,lcsh:Medicine ,Translation (biology) ,Biology ,Mitochondrion ,Article ,Mitochondria ,Cell biology ,Mitochondrial Proteins ,Protein Biosynthesis ,biology.protein ,Protein biosynthesis ,Humans ,Initiation factor ,lcsh:Q ,Eukaryotic Initiation Factors ,lcsh:Science ,Functional divergence ,HeLa Cells - Abstract
The initiation of protein synthesis in bacteria is ruled by three canonical factors: IF1, IF2, and IF3. This system persists in human mitochondria; however, it functions in a rather different way due to specialization and adaptation to the organellar micro-environment. We focused on human mitochondrial IF3, which was earlier studied in vitro, but no knock-out cellular models have been published up to date. In this work, we generated human HeLa cell lines deficient in the MTIF3 gene and analyzed their mitochondrial function. Despite the lack of IF3mt in these cells, they preserved functional mitochondria capable of oxygen consumption and protein synthesis; however, the translation of ATP6 mRNA was selectively decreased which compromised the assembly of ATP synthase. Together with the analogous results obtained earlier for baker’s yeast mitochondrial IF3, our findings point to a functional divergence of mitochondrial initiation factors from their bacterial ancestors.
- Published
- 2020
16. Yeast Mitochondrial Translation Initiation Factor 3 Interacts with Pet111p to Promote COX2 mRNA Translation
- Author
-
S. A. Levitskii, Piotr Kamenski, I. V. Chicherin, Maria V. Baleva, Igor A. Krasheninnikov, and M. V. Patrushev
- Subjects
0301 basic medicine ,Mitochondrial translation ,Respiratory chain ,translation ,Mitochondrion ,Biology ,Catalysis ,lcsh:Chemistry ,Inorganic Chemistry ,03 medical and health sciences ,chemistry.chemical_compound ,Biosynthesis ,initiation factor ,Protein biosynthesis ,Initiation factor ,Physical and Theoretical Chemistry ,lcsh:QH301-705.5 ,Molecular Biology ,Spectroscopy ,030102 biochemistry & molecular biology ,Organic Chemistry ,Translation (biology) ,General Medicine ,Yeast ,Computer Science Applications ,Cell biology ,mitochondria ,030104 developmental biology ,lcsh:Biology (General) ,lcsh:QD1-999 ,chemistry ,translational activator - Abstract
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.
- Published
- 2020
17. 60S dynamic state of bacterial ribosome is fixed by yeast mitochondrial initiation factor 3
- Author
-
Ksenia Derbikova, S. A. Levitskii, Maria V. Baleva, Andrey V. Golovin, Igor A. Krasheninnikov, Anton Kuzmenko, Piotr Kamenski, and I. V. Chicherin
- Subjects
0301 basic medicine ,Translation ,Saccharomyces cerevisiae ,lcsh:Medicine ,Mitochondrion ,medicine.disease_cause ,Ribosome ,General Biochemistry, Genetics and Molecular Biology ,03 medical and health sciences ,Initiation factor 3 ,Protein biosynthesis ,medicine ,Initiation factor ,Escherichia coli ,biology ,Chemistry ,Eukaryotic Large Ribosomal Subunit ,General Neuroscience ,lcsh:R ,Subunit dissociation ,General Medicine ,Ribosomal RNA ,biology.organism_classification ,Cell biology ,030104 developmental biology ,General Agricultural and Biological Sciences - Abstract
The processes of association and dissociation of ribosomal subunits are of great importance for the protein biosynthesis. The mechanistic details of these processes, however, are not well known. In bacteria, upon translation termination, the ribosome dissociates into subunits which is necessary for its further involvement into new initiation step. The dissociated state of the ribosome is maintained by initiation factor 3 (IF3) which binds to free small subunits and prevents their premature association with large subunits. In this work, we have exchanged IF3 inEscherichia colicells by its ortholog fromSaccharomyces cerevisiaemitochondria (Aim23p) and showed that yeast protein cannot functionally substitute the bacterial one and is even slightly toxic for bacterial cells. Our in vitro experiments have demonstrated that Aim23p does not splitE. coliribosomes into subunits. Instead, it fixes a state of ribosomes characterized by sedimentation coefficient about 60S which is not a stable structure but rather reflects a shift of dynamic equilibrium between associated and dissociated states of the ribosome. Mitochondria-specific terminal extensions of Aim23p are necessary for “60S state” formation, and molecular modeling results point out that these extensions might stabilize the position of the protein on the bacterial ribosome.
- Published
- 2018
18. Biological and Evolutionary Significance of Terminal Extensions of Mitochondrial Translation Initiation Factor 3
- Author
-
I. V. Chicherin, Anton Kuzmenko, Maria Klimontova, Piotr Kamenski, S. A. Levitskii, Maria V. Baleva, Igor A. Krasheninnikov, and Ksenia Derbikova
- Subjects
0301 basic medicine ,Saccharomyces cerevisiae Proteins ,Mitochondrial translation ,translation ,Prokaryotic Initiation Factor-3 ,Saccharomyces cerevisiae ,Biology ,Mitochondrion ,Article ,Catalysis ,lcsh:Chemistry ,Evolution, Molecular ,Inorganic Chemistry ,terminal extension ,03 medical and health sciences ,Protein Domains ,initiation factor ,Escherichia coli ,Protein biosynthesis ,Humans ,Initiation factor ,Translation factor ,Physical and Theoretical Chemistry ,lcsh:QH301-705.5 ,Molecular Biology ,Spectroscopy ,Organic Chemistry ,Translation (biology) ,General Medicine ,Fusion protein ,initiation ,Mitochondria ,Computer Science Applications ,Cell biology ,030104 developmental biology ,lcsh:Biology (General) ,lcsh:QD1-999 ,Function (biology) - Abstract
Protein biosynthesis in mitochondria is organized in a bacterial manner. However, during evolution, mitochondrial translation mechanisms underwent many organelle-specific changes. In particular, almost all mitochondrial translation factors, being orthologous to bacterial proteins, are characterized by some unique elements of primary or secondary structure. In the case of the organellar initiation factor 3 (IF3), these elements are several dozen amino acids long N- and C-terminal extensions. This study focused on the terminal extensions of baker&rsquo, s yeast mitochondrial IF3, Aim23p. By in vivo deletion and complementation analysis, we show that at least one extension is necessary for Aim23p function. At the same time, human mitochondrial IF3 is fully functional in yeast mitochondria even without both terminal extensions. While Escherichia coli IF3 itself is poorly active in yeast mitochondria, adding Aim23p terminal extensions makes the resulting chimeric protein as functional as the cognate factor. Our results show that the terminal extensions of IF3 have evolved as the &ldquo, adaptors&rdquo, that accommodate the translation factor of bacterial origin to the evolutionary changed protein biosynthesis system in mitochondria.
- Published
- 2018
19. Aim23p Interacts with the Yeast Mitochondrial Ribosomal Small Subunit.
- Author
-
Chicherin, I. V., Zinina, V. V., Levitskiy, S. A., Serebryakova, M. V., and Kamenski, P. A.
- Subjects
YEAST physiology ,MITOCHONDRIA ,PROTEIN synthesis ,RIBOSOMES ,GENETIC translation ,INITIATION factors (Biochemistry) ,IMMUNOPRECIPITATION - Abstract
Protein synthesis in mitochondria is generally organized in a bacterial-like manner but, at the same time, possesses several unique traits. Translation initiation in mitochondria is regulated by two protein factors, mtIF2 and mtIF3. Previously we demonstrated that Saccharomyces cerevisiae Aim23 protein is an ortholog of IF3 in budding yeast. However, the data on the interactions between Aim23p and other proteins are limited. Here, we demonstrated that Aim23p interacts with the yeast mitochondrial ribosomal small subunit both in vivo and in vitro using co-immunoprecipitation and density gradient sedimentation. [ABSTRACT FROM AUTHOR]
- Published
- 2019
- Full Text
- View/download PDF
20. 60S dynamic state of bacterial ribosome is fixed by yeast mitochondrial initiation factor 3.
- Author
-
Levitskii, Sergey, Derbikova, Ksenia, Baleva, Maria V., Kuzmenko, Anton, Golovin, Andrey V., Chicherin, Ivan, Krasheninnikov, Igor A., and Kamenski, Piotr
- Subjects
RIBOSOMES ,BACTERIAL proteins ,YEAST ,PROTEIN synthesis ,BACTERIAL cells ,SACCHAROMYCES cerevisiae ,ESCHERICHIA coli - Abstract
The processes of association and dissociation of ribosomal subunits are of great importance for the protein biosynthesis. The mechanistic details of these processes, however, are not well known. In bacteria, upon translation termination, the ribosome dissociates into subunits which is necessary for its further involvement into new initiation step. The dissociated state of the ribosome is maintained by initiation factor 3 (IF3) which binds to free small subunits and prevents their premature association with large subunits. In this work, we have exchanged IF3 in Escherichia coli cells by its ortholog from Saccharomyces cerevisiae mitochondria (Aim23p) and showed that yeast protein cannot functionally substitute the bacterial one and is even slightly toxic for bacterial cells. Our in vitro experiments have demonstrated that Aim23p does not split E. coli ribosomes into subunits. Instead, it fixes a state of ribosomes characterized by sedimentation coefficient about 60S which is not a stable structure but rather reflects a shift of dynamic equilibrium between associated and dissociated states of the ribosome. Mitochondria-specific terminal extensions of Aim23p are necessary for "60S state" formation, and molecular modeling results point out that these extensions might stabilize the position of the protein on the bacterial ribosome. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
21. Yeast Mitochondrial Translation Initiation Factor 3 Interacts with Pet111p to Promote COX2 mRNA Translation.
- Author
-
Chicherin, Ivan, Levitskii, Sergey, Baleva, Maria V., Krasheninnikov, Igor A., Patrushev, Maxim V., and Kamenski, Piotr
- Subjects
YEAST ,MESSENGER RNA ,MATHEMATICAL complexes ,POTYVIRUSES ,MITOCHONDRIAL proteins ,TRANSLATIONS ,PLANT mitochondria - Abstract
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. [ABSTRACT FROM AUTHOR]
- Published
- 2020
- Full Text
- View/download PDF
22. Biological and Evolutionary Significance of Terminal Extensions of Mitochondrial Translation Initiation Factor 3.
- Author
-
Derbikova, Ksenia, Kuzmenko, Anton, Levitskii, Sergey, Klimontova, Maria, Chicherin, Ivan, Baleva, Maria V., Krasheninnikov, Igor A., and Kamenski, Piotr
- Subjects
PROTEIN synthesis ,BACTERIA ,AMINO acids ,YEAST ,MITOCHONDRIA ,ESCHERICHIA coli - Abstract
Protein biosynthesis in mitochondria is organized in a bacterial manner. However, during evolution, mitochondrial translation mechanisms underwent many organelle-specific changes. In particular, almost all mitochondrial translation factors, being orthologous to bacterial proteins, are characterized by some unique elements of primary or secondary structure. In the case of the organellar initiation factor 3 (IF3), these elements are several dozen amino acids long N- and C-terminal extensions. This study focused on the terminal extensions of baker's yeast mitochondrial IF3, Aim23p. By in vivo deletion and complementation analysis, we show that at least one extension is necessary for Aim23p function. At the same time, human mitochondrial IF3 is fully functional in yeast mitochondria even without both terminal extensions. While Escherichia coli IF3 itself is poorly active in yeast mitochondria, adding Aim23p terminal extensions makes the resulting chimeric protein as functional as the cognate factor. Our results show that the terminal extensions of IF3 have evolved as the "adaptors" that accommodate the translation factor of bacterial origin to the evolutionary changed protein biosynthesis system in mitochondria. [ABSTRACT FROM AUTHOR]
- Published
- 2018
- Full Text
- View/download PDF
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