60S dynamic state of bacterial ribosome is fixed by Yeast mitochondrial initiation factor 3
Levitskii S., Derbikova K., Baleva M. V., Kuzmenko A., Golovin A. V., Chicherin I., Krasheninnikov I. A., Kamenski P.
PeerJ
Vol.2018, Issue9, Num.e5620
Опубликовано: 2018
Тип ресурса: Статья
Аннотация:
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 stabl
Ключевые слова:
Initiation factor 3; Ribosome; Subunit dissociation; Translation
bacterial protein; initiation factor 3; oligonucleotide; 60S ribosomal subunit; Article; bacterial cell; bacterial strain; Escherichia coli; mitochondrion; molecular model; nonhuman; polymerase chain reaction; promoter region; protein analysis; protein interaction; protein purification; protein synthesis; Saccharomyces cerevisiae; sedimentation; translation termination; yeast
Язык текста: Английский
ISSN: 2167-8359
Levitskii S.
Derbikova K.
Baleva M. V.
Kuzmenko A.
Golovin A. V. Andrej Viktorovich 1975-
Chicherin I.
Krasheninnikov I. A.
Kamenski P.
Левицкии С.
Дербикова К.
Балева М. В.
Кузменко А.
Головин А. В. Андрей Викторович 1975-
Чичерин И.
Крашенинников И. А.
Каменски П.
60S dynamic state of bacterial ribosome is fixed by Yeast mitochondrial initiation factor 3
Текст визуальный непосредственный
PeerJ
Vol.2018, Issue9 Num.e5620
2018
Статья
Initiation factor 3 Ribosome Subunit dissociation Translation
bacterial protein initiation factor 3 oligonucleotide 60S ribosomal subunit Article bacterial cell bacterial strain Escherichia coli mitochondrion molecular model nonhuman polymerase chain reaction promoter region protein analysis protein interaction protein purification protein synthesis Saccharomyces cerevisiae sedimentation translation termination yeast
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 stabl