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Heterogeneity of the translational machinery: Variations on a common theme.
- Source :
-
Biochimie [Biochimie] 2015 Jul; Vol. 114, pp. 39-47. Date of Electronic Publication: 2014 Dec 24. - Publication Year :
- 2015
-
Abstract
- In all organisms the universal process of protein synthesis is performed by the ribosome, a complex multi-component assembly composed of RNA and protein elements. Although ribosome heterogeneity was observed already more than 40 years ago, the ribosome is still traditionally viewed as an unchangeable entity that has to be equipped with all ribosomal components and translation factors in order to precisely accomplish all steps in protein synthesis. In the recent years this concept was challenged by several studies highlighting a broad variation in the composition of the translational machinery in response to environmental signals, which leads to its adaptation and functional specialization. Here, we summarize recent reports on the variability of the protein synthesis apparatus in diverse organisms and discuss the multiple mechanisms and possibilities that can lead to functional ribosome heterogeneity. Collectively, these results indicate that all cells are equipped with a remarkable toolbox to fine tune gene expression at the level of translation and emphasize the physiological importance of ribosome heterogeneity for the immediate implementation of environmental information.<br /> (Copyright © 2015 The Authors. Published by Elsevier B.V. All rights reserved.)
- Subjects :
- Animals
Gene Expression Regulation
Humans
Peptide Initiation Factors physiology
Protein Processing, Post-Translational
RNA Processing, Post-Transcriptional
RNA, Ribosomal physiology
RNA, Transfer physiology
Ribosomal Proteins physiology
Stress, Physiological
Protein Biosynthesis
Ribosomes physiology
Subjects
Details
- Language :
- English
- ISSN :
- 1638-6183
- Volume :
- 114
- Database :
- MEDLINE
- Journal :
- Biochimie
- Publication Type :
- Academic Journal
- Accession number :
- 25542647
- Full Text :
- https://doi.org/10.1016/j.biochi.2014.12.011