The Role of Ribosome and TRNA Dynamics in the Regulation of Translation Elongation PDF Download
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Author: Wei Ning
Publisher:
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Languages : en
Pages :
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Protein synthesis, one of nature's most fundamental processes within all living cells, is catalyzed by the ribosome, a highly conserved, massive, two-subunit ribonucleoprotein complex. Ribosomes synthesize proteins based on the sequence of triplet-nucleotide codons presented by the messenger RNA (mRNA) template, using aminoacyl-transfer RNAs (aa-tRNAs) substrates, which deliver individual amino acids to the ribosome. Recent biochemical, structural, dynamic and computational studies have uncovered large-scale conformational changes of the ribosome, its tRNA substrates, and translation factors that play important roles in regulating protein synthesis, especially during the elongation phase of translation. For example, translocation of the ribosome along its mRNA template involves several conformational rearrangements of the ribosomal pre-translocation (PRE) complex, including the rotation of two ribosomal subunits, closure of the L1 stalk element, and reconfigurations of the ribosome-bound tRNAs.
Author: Wei Ning
Publisher:
ISBN:
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Languages : en
Pages :
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Book Description
Protein synthesis, one of nature's most fundamental processes within all living cells, is catalyzed by the ribosome, a highly conserved, massive, two-subunit ribonucleoprotein complex. Ribosomes synthesize proteins based on the sequence of triplet-nucleotide codons presented by the messenger RNA (mRNA) template, using aminoacyl-transfer RNAs (aa-tRNAs) substrates, which deliver individual amino acids to the ribosome. Recent biochemical, structural, dynamic and computational studies have uncovered large-scale conformational changes of the ribosome, its tRNA substrates, and translation factors that play important roles in regulating protein synthesis, especially during the elongation phase of translation. For example, translocation of the ribosome along its mRNA template involves several conformational rearrangements of the ribosomal pre-translocation (PRE) complex, including the rotation of two ribosomal subunits, closure of the L1 stalk element, and reconfigurations of the ribosome-bound tRNAs.
Author: Heinz Bielka
Publisher: Walter de Gruyter GmbH & Co KG
ISBN: 3112729757
Category : Science
Languages : en
Pages : 340
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No detailed description available for "The Eukaryotic Ribosome".
Author: Albert Tsai
Publisher:
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Languages : en
Pages :
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Translation is the final step that converts genetic information into proteins composed of amino acids using the ribosome-- a complex molecular machine that coordinates the kinetics, chemistry, and mechanics necessary to synthesize a polypeptide. Translation is highly dynamic with processes taking place on the microseconds to minutes timescales. Among the different techniques employed to probe the dynamics of translation, single-molecule fluorescence occupies a unique position, being able to track heterogeneous compositional and conformational changes occurring within tens of milliseconds to minutes. Leveraging several fluorescent signals, we probed the dynamics of translation initiation. Instead of a linear pathway, we observed several different pathways all leading to the formation of an elongation competent ribosome complex, with the flux through each modulated by initiation factors, tRNAs, and mRNA sequence. Next, we tracked how the aminoglycoside family of antibiotics inhibits ribosome and tRNA dynamics during peptide synthesis (elongation), concluding that their potency as bactericides stems from kinetically inhibiting elongation. Finally, we transitioned from model systems into observing elongation dynamics on a biologically functional protein stall sequence, SecM. Our results suggest that stalling the ribosome requires several precisely-timed peptide-ribosome interactions and that ribosomes stall in a distribution of locations on the SecM sequence. These results demonstrate the power of single-molecule fluorescence to monitor global translation dynamics, as well as highlighting the importance of the temporal dimension in forming a coherent and global mechanism for translation.
Author: Marina V. Rodnina
Publisher: Springer Science & Business Media
ISBN: 3709102154
Category : Medical
Languages : en
Pages : 428
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Book Description
The ribosome is a macromolecular machine that synthesizes proteins with a high degree of speed and accuracy. Our present understanding of its structure, function and dynamics is the result of six decades of research. This book collects over 40 articles based on the talks presented at the 2010 Ribosome Meeting, held in Orvieto, Italy, covering all facets of the structure and function of the ribosome. New high-resolution crystal structures of functional ribosome complexes and cryo-EM structures of translating ribosomes are presented, while partial reactions of translation are examined in structural and mechanistic detail, featuring translocation as a most dynamic process. Mechanisms of initiation, both in bacterial and eukaryotic systems, translation termination, and novel details of the functions of the respective factors are described. Structure and interactions of the nascent peptide within, and emerging from, the ribosomal peptide exit tunnel are addressed in several articles. Structural and single-molecule studies reveal a picture of the ribosome exhibiting the energy landscape of a processive Brownian machine. The collection provides up-to-date reviews which will serve as a source of essential information for years to come.
Author: Qi Liu
Publisher:
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Languages : en
Pages :
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Abstract: The ribosome performs the essential function of protein synthesis in all living cells. The major functional form of bacterial ribosomes is a 70S complex, which is composed of two subunits, 30S and 50S. The interactions between the two subunits are clustered into several regions of the subunit interface and referred to as intersubunit bridges. Bridge interactions form during the subunit-joining step of translation initiation, which is critical for establishing the open reading frame of translation, while disruption of bridges during ribosome recycling helps to return both subunits into the translating pool. For the translation machinery to move along the messenger RNA (mRNA), bridges undergo large-scale rearrangement during each cycle of translation elongation. Therefore, the structure and dynamics of intersubunit bridges are crucial for ribosomal functions.
Author: Antonius M. VanDongen
Publisher: CRC Press
ISBN: 142004415X
Category : Medical
Languages : en
Pages : 368
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Book Description
The NMDA receptor plays a critical role in the development of the central nervous system and in adult neuroplasticity, learning, and memory. Therefore, it is not surprising that this receptor has been widely studied. However, despite the importance of rhythms for the sustenance of life, this aspect of NMDAR function remains poorly studied. Written
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Languages : en
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Like most biological polymerization reactions, ribosome-catalyzed protein synthesis, or translation, can be divided into initiation, elongation, and termination stages. Initiation is the rate-limiting stage of translation and a critical site for translational control of gene expression. Throughout all stages of protein synthesis, the ribosome is aided by essential protein co-factors known as translation factors. I have studied the role that two translation initiation factors, IF1 and IF3, play in the mechanism and regulation of translation initiation in Escherichia coli. Specifically, I have used single-molecule fluorescence resonance energy transfer (smFRET) as a primary tool for investigating how the dynamics of IF1 and IF3 regulate the accuracy with which the translational machinery selects an initiator transfer RNA (tRNA) and the correct messenger RNA (mRNA) start codon during the initiation stage of protein synthesis.
Author: James B. Munro
Publisher:
ISBN:
Category :
Languages : en
Pages : 548
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Author: Ernest Frederick Gale
Publisher: John Wiley & Sons
ISBN:
Category : Medical
Languages : en
Pages : 682
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Author: Dongli Pan
Publisher:
ISBN:
Category :
Languages : en
Pages : 207
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