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Izvestiia Akademii Nauk SSSR. Seriia... 1965
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Annual Review of Biochemistry 1958
Topics: Protein Biosynthesis; Proteins
PubMed: 13571928
DOI: 10.1146/annurev.bi.27.070158.000343 -
Annual Review of Genetics 1970
Review
Topics: Escherichia coli; Genes; Mutation; Peptide Chain Elongation, Translational; Peptide Chain Termination, Translational; Phenotype; Protein Biosynthesis; RNA, Transfer; Ribosomes; Suppression, Genetic
PubMed: 4950057
DOI: 10.1146/annurev.ge.04.120170.000543 -
Current Opinion in Cell Biology Jun 2001Nuclear RNA-binding proteins can record pre-mRNA processing events in the structure of messenger ribonucleoprotein particles (mRNPs). During initial rounds of... (Review)
Review
Nuclear RNA-binding proteins can record pre-mRNA processing events in the structure of messenger ribonucleoprotein particles (mRNPs). During initial rounds of translation, the mature mRNP structure is established and is monitored by mRNA surveillance systems. Competition for the cap structure links translation and subsequent mRNA degradation, which may also involve multiple deadenylases.
Topics: Alternative Splicing; Animals; Peptide Chain Initiation, Translational; Protein Biosynthesis; RNA Precursors; RNA, Messenger; Ribonucleases; Ribonucleoproteins; Yeasts
PubMed: 11343902
DOI: 10.1016/s0955-0674(00)00214-3 -
The Journal of Biological Chemistry Jul 2020Bacteria must rapidly respond to both intracellular and environmental changes to survive. One critical mechanism to rapidly detect and adapt to changes in environmental... (Review)
Review
Bacteria must rapidly respond to both intracellular and environmental changes to survive. One critical mechanism to rapidly detect and adapt to changes in environmental conditions is control of gene expression at the level of protein synthesis. At each of the three major steps of translation-initiation, elongation, and termination-cells use stimuli to tune translation rate and cellular protein concentrations. For example, changes in nutrient concentrations in the cell can lead to translational responses involving mechanisms such as dynamic folding of riboswitches during translation initiation or the synthesis of alarmones, which drastically alter cell physiology. Moreover, the cell can fine-tune the levels of specific protein products using programmed ribosome pausing or inducing frameshifting. Recent studies have improved understanding and revealed greater complexity regarding long-standing paradigms describing key regulatory steps of translation such as start-site selection and the coupling of transcription and translation. In this review, we describe how bacteria regulate their gene expression at the three translational steps and discuss how translation is used to detect and respond to changes in the cellular environment. Finally, we appraise the costs and benefits of regulation at the translational level in bacteria.
Topics: Adaptation, Physiological; Bacteria; Bacterial Proteins; Protein Biosynthesis
PubMed: 32518156
DOI: 10.1074/jbc.REV120.012742 -
Proceedings of the National Academy of... Jun 2020Split inteins are privileged molecular scaffolds for the chemical modification of proteins. Though efficient for in vitro applications, these polypeptide ligases have...
Split inteins are privileged molecular scaffolds for the chemical modification of proteins. Though efficient for in vitro applications, these polypeptide ligases have not been utilized for the semisynthesis of proteins in live cells. Here, we biochemically and structurally characterize the naturally split intein VidaL. We show that this split intein, which features the shortest known N-terminal fragment, supports rapid and efficient protein -splicing under a range of conditions, enabling semisynthesis of modified proteins both in vitro and in mammalian cells. The utility of this protein engineering system is illustrated through the traceless assembly of multidomain proteins whose biophysical properties render them incompatible with a single expression system, as well as by the semisynthesis of dual posttranslationally modified histone proteins in live cells. We also exploit the domain swapping function of VidaL to effect simultaneous modification and translocation of the nuclear protein HP1α in live cells. Collectively, our studies highlight the VidaL system as a tool for the precise chemical modification of cellular proteins with spatial and temporal control.
Topics: Cell Engineering; Inteins; Protein Biosynthesis; Protein Engineering; Protein Splicing
PubMed: 32424098
DOI: 10.1073/pnas.2003613117 -
The Journal of Biological Chemistry Oct 2011The specific inhibition of the biosynthesis of target proteins is a relatively novel strategy in pharmacology and is based mainly on antisense approaches (e.g. antisense...
The specific inhibition of the biosynthesis of target proteins is a relatively novel strategy in pharmacology and is based mainly on antisense approaches (e.g. antisense oligonucleotides or RNA interference). Recently, a novel class of substances was described acting at a later step of protein biosynthesis. The cyclic heptadepsipeptides CAM741 and cotransin were shown to inhibit selectively the biosynthesis of a small subset of secretory proteins by preventing stable insertion of the nascent chains into the Sec61 translocon complex at the endoplasmic reticulum membrane (Besemer, J., Harant, H., Wang, S., Oberhauser, B., Marquardt, K., Foster, C. A., Schreiner, E. P., de Vries, J. E., Dascher-Nadel, C., and Lindley, I. J. (2005) Nature 436, 290-293; Garrison, J. L., Kunkel, E. J., Hegde, R. S., and Taunton, J. (2005) Nature 436, 285-289). These peptides act in a signal sequence-discriminatory manner, which explains their selectivity. Here, we have analyzed the cotransin sensitivity of various G protein-coupled receptors in transfected HEK 293 cells. We show that the biosynthesis of the human endothelin B receptor (ET(B)R) is highly sensitive to cotransin, in contrast to that of the other G protein-coupled receptors analyzed. Using a novel biosynthesis assay based on fusions with the photoconvertible Kaede protein, we show that the IC(50) value of cotransin action on ET(B)R biosynthesis is 5.4 μm and that ET(B)R signaling could be completely blocked by treating cells with 30 μm cotransin. Taken together, our data add an integral membrane protein, namely the ET(B)R, to the small group of cotransin-sensitive proteins.
Topics: HEK293 Cells; Humans; Luminescent Proteins; Peptides, Cyclic; Protein Biosynthesis; Receptor, Endothelin B; Recombinant Fusion Proteins
PubMed: 21808059
DOI: 10.1074/jbc.M111.239244 -
Journal of Molecular Biology May 2016The ribosome is a large two-subunit ribonucleoprotein machine that translates the genetic code in all cells, synthesizing proteins according to the sequence of the mRNA... (Review)
Review
The ribosome is a large two-subunit ribonucleoprotein machine that translates the genetic code in all cells, synthesizing proteins according to the sequence of the mRNA template. During translation, the primary substrates, transfer RNAs, pass through binding sites formed between the two subunits. Multiple interactions between the ribosomal subunits, termed intersubunit bridges, keep the ribosome intact and at the same time govern dynamics that facilitate the various steps of translation such as transfer RNA-mRNA movement. Here, we review the molecular nature of these intersubunit bridges, how they change conformation during translation, and their functional roles in the process.
Topics: Protein Biosynthesis; RNA, Messenger; RNA, Transfer; Ribosomes
PubMed: 26880335
DOI: 10.1016/j.jmb.2016.02.009 -
The Proceedings of the Nutrition Society 1945
Topics: Protein Biosynthesis
PubMed: 21004646
DOI: 10.1017/s0029665145000107 -
Nature Chemical Biology Apr 2021Coupled transcription and translation processes in bacteria cause indiscriminate translation of intact and truncated messenger RNAs, inevitably generating nonfunctional...
Coupled transcription and translation processes in bacteria cause indiscriminate translation of intact and truncated messenger RNAs, inevitably generating nonfunctional polypeptides. Here, we devised a synthetic protein quality control (ProQC) system that enables translation only when both ends of mRNAs are present and followed by circularization based on sequence-specific RNA-RNA hybridization. We demonstrate that the ProQC system dramatically improved the fraction of full-length proteins among all synthesized polypeptides by selectively translating intact mRNA and reducing abortive translation. As a result, full-length protein synthesis increased up to 2.5-fold without changing the transcription or translation efficiency. Furthermore, we applied the ProQC system for 3-hydroxypropionic acid, violacein and lycopene production by ensuring full-length expression of enzymes in biosynthetic pathways, resulting in 1.6- to 2.3-fold greater biochemical production. We believe that our ProQC system can be universally applied to improve not only the quality of recombinant protein production but also efficiencies of metabolic pathways.
Topics: Bacteria; Base Sequence; Escherichia coli; Genetic Engineering; Peptides; Protein Biosynthesis; Proteins; Quality Control; RNA, Messenger
PubMed: 33542534
DOI: 10.1038/s41589-021-00736-3