scholarly journals Mechanisms of elongation on the ribosome: dynamics of a macromolecular machine

2004 ◽  
Vol 32 (5) ◽  
pp. 733-737 ◽  
Author(s):  
W. Wintermeyer ◽  
F. Peske ◽  
M. Beringer ◽  
K.B. Gromadski ◽  
A. Savelsbergh ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Kinetic Analysis ◽  
Recent Progress ◽  
Structural Data ◽  
Rna Molecules ◽  
Ribonucleoprotein Particles ◽  
Elongation Phase

Protein synthesis in the cell is performed on ribosomes, large ribonucleoprotein particles, which in bacteria consist of three RNA molecules and over 50 proteins. This review summarizes recent progress in understanding the mechanisms of the elongation phase of protein synthesis. Results from rapid kinetic analysis of elongation reactions are discussed in the light of recent structural data.

scholarly journals Effects on protein synthesis of injecting synthetic polyribonucleotides into living cells

1974 ◽  
Vol 144 (1) ◽  
pp. 11-19 ◽  
Author(s):  
Hugh Woodland ◽  
Sarah E. Ayers
Keyword(s):  
Protein Synthesis ◽  
Xenopus Laevis ◽  
Potent Inhibitor ◽  
Living Cells ◽  
Initiation Factor ◽  
Rna Molecules ◽  
Endogenous Protein ◽  
Limited Supply ◽  
Inhibitor Of Protein Synthesis ◽  
Haemoglobin Synthesis

Micro-injection into the oocytes and eggs of Xenopus laevis was used to ascertain the effects of synthetic polyribonucleotides on protein synthesis in living cells. Poly(U) and poly(A) were not translated detectably, nor did they change the rate of endogenous protein synthesis. The same was true of poly(G,U), poly(A,G,U), poly(A,C,G,U), G-U-G-(U)n, A-(U)n and AUG. In contrast, A-U-G-(U)n was a potent inhibitor of protein synthesis in the cell. This might be because it is initiated normally but lacks a termination codon, or because it inhibits the translation of other molecules in some way not dependent on its normal initiation. Poly(G,U), poly(A,G,U) and poly(A,C,G,U) inhibited haemoglobin synthesis when they were injected into the oocyte with haemoglobin mRNA. The synthetic polyribonucleotides did not inhibit the translation of the natural mRNA when the two sorts of molecules were injected at different times. It is suggested that the synthetic RNA molecules compete with the natural mRNA for a pre-initiation factor in limited supply.

scholarly journals Recent progress in microstructural hydrogen mapping in steels: quantification, kinetic analysis, and multi-scale characterisation

2017 ◽  
Vol 33 (13) ◽  
pp. 1481-1496 ◽  
Author(s):  
Motomichi Koyama ◽  
Michael Rohwerder ◽  
Cemal Cem Tasan ◽  
Asif Bashir ◽  
Eiji Akiyama ◽  
...  
Keyword(s):  
Kinetic Analysis ◽  
Recent Progress ◽  
Multi Scale

Fluoride exposure regulates the elongation phase of protein synthesis in cultured Bergmann glia cells

2014 ◽  
Vol 229 (1) ◽  
pp. 126-133 ◽  
Author(s):  
Marco Flores-Méndez ◽  
Diana Ramírez ◽  
Nely Alamillo ◽  
Luisa C. Hernández-Kelly ◽  
Luz María Del Razo ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Bergmann Glia ◽  
Glia Cells ◽  
Fluoride Exposure ◽  
Elongation Phase

scholarly journals Walking around Ribosomal Small Subunit: A Possible “Tourist Map” for Electron Holes

Molecules ◽  
2021 ◽  
Vol 26 (18) ◽  
pp. 5479
Author(s):  
Andrey Yu. Sosorev
Keyword(s):  
Protein Synthesis ◽  
Molecular Biology ◽  
Small Subunit ◽  
Translation Process ◽  
Subunit A ◽  
Rna Molecules ◽  
Charge Localization ◽  
Allosteric Mechanism ◽  
Electron Holes ◽  
Hole Localization

Despite several decades of research, the physics underlying translation—protein synthesis at the ribosome—remains poorly studied. For instance, the mechanism coordinating various events occurring in distant parts of the ribosome is unknown. Very recently, we suggested that this allosteric mechanism could be based on the transport of electric charges (electron holes) along RNA molecules and localization of these charges in the functionally important areas; this assumption was justified using tRNA as an example. In this study, we turn to the ribosome and show computationally that holes can also efficiently migrate within the whole ribosomal small subunit (SSU). The potential sites of charge localization in SSU are revealed, and it is shown that most of them are located in the functionally important areas of the ribosome—intersubunit bridges, Fe4S4 cluster, and the pivot linking the SSU head to its body. As a result, we suppose that hole localization within the SSU can affect intersubunit rotation (ratcheting) and SSU head swiveling, in agreement with the scenario of electronic coordination of ribosome operation. We anticipate that our findings will improve the understanding of the translation process and advance molecular biology and medicine.

scholarly journals Walking Around Ribosomal Small Subunit: A Possible “Tourist Map” for an Electron Hole

2021 ◽  
Author(s):  
Andrey Yu. Sosorev
Keyword(s):  
Protein Synthesis ◽  
Small Subunit ◽  
The Body ◽  
Translation Process ◽  
Electron Hole ◽  
Rna Molecules ◽  
Charge Localization ◽  
Allosteric Mechanism ◽  
Electron Holes ◽  
Hole Localization

Despite several decades of research, the physics underlying translation – protein synthesis at the ribosome – remains poorly studied. For instance, the mechanism coordinating various events occurring in distant parts of the ribosome is unknown. Very recently, we have suggested that this allosteric mechanism could be based on the transport of electric charges (electron holes) along RNA molecules and localization of these charges in the functionally important areas; this assumption was justified using tRNA as an example. In this study, we turn to the ribosome and show computationally that holes can also efficiently migrate within the whole ribosomal small subunit (SSU). The potential sites of charge localization in SSU are revealed, and it is shown that most of them are located in the functionally important areas of the ribosome – intersubunit bridges, Fe4S4 cluster and the pivot linking the SSU head to the body. As a result, we suppose that hole localization within the SSU can affect intersubunit rotation (ratcheting) and SSU head swiveling, in agreement with the scenario of electronic coordination of ribosome operation. We anticipate that our findings will improve the understanding of the translation process and advance the molecular biology and medicine.

scholarly journals Stage-specific synthesis of proteins complexed to ribonucleoprotein particles and ribosomes in zoospores of Blastocladiella emersonii.

1981 ◽  
Vol 1 (4) ◽  
pp. 310-320 ◽  
Author(s):  
A J Jaworski ◽  
P Stumhofer
Keyword(s):  
Protein Synthesis ◽  
Ribonucleic Acid ◽  
Gel Electrophoresis ◽  
Molecular Weights ◽  
Ribonucleoprotein Particles ◽  
Blastocladiella Emersonii ◽  
Specific Synthesis

In Blastocladiella emersonii zoospores, a set of proteins was found associated with the ribosomes and free ribonucleoprotein particles distinct from the ribosomes and polyribosomes. These proteins were designated P120, P105, P64, P56, and P42 based on their molecular weights determined by gel electrophoresis. Synthesis of these proteins was detected only during late sporulation just before the time polyadenylated ribonucleic acid accumulates in the sporangia. These proteins banded in isopycnic metrizamide gradients at densities of 1.31 and 1.27 g/cm3, which corresponded to the densities of the ribosomes and free ribonucleoprotein particles, respectively. Comparison of the distribution of the proteins in sucrose versus metrizamide gradients suggested that P105 was removed from the free ribonucleoprotein particles before complexing with the ribosomes. During germination, these proteins disappeared from the ribosomal fractions, with kinetics corresponding to the resumption of protein synthesis. Another protein (P178) was observed to bind to the ribosomes before the onset of protein synthesis during germination. Cycloheximide did not block the addition of this protein to the monoribosomes.

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