Regulation of Protein Synthesis via the Network Between Modified Nucleotides in tRNA and tRNA Modification Enzymes in Thermus thermophilus, a Thermophilic Eubacterium

2016 ◽  
pp. 73-89
Author(s):  
Hiroyuki Hori ◽  
Ryota Yamagami ◽  
Chie Tomikawa
Keyword(s):  
Protein Synthesis ◽  
Thermus Thermophilus ◽  
Trna Modification ◽  
Modified Nucleotides

scholarly journals Transfer RNA Modification Enzymes from Thermophiles and Their Modified Nucleosides in tRNA

2018 ◽  
Vol 6 (4) ◽  
pp. 110 ◽  
Author(s):  
Hiroyuki Hori ◽  
Takuya Kawamura ◽  
Takako Awai ◽  
Anna Ochi ◽  
Ryota Yamagami ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
High Temperatures ◽  
Rna Binding ◽  
Rna Binding Proteins ◽  
Thermus Thermophilus ◽  
Medical Science ◽  
Modified Nucleosides ◽  
Rna Modification ◽  
Trna Modification ◽  
Response To Temperature

To date, numerous modified nucleosides in tRNA as well as tRNA modification enzymes have been identified not only in thermophiles but also in mesophiles. Because most modified nucleosides in tRNA from thermophiles are common to those in tRNA from mesophiles, they are considered to work essentially in steps of protein synthesis at high temperatures. At high temperatures, the structure of unmodified tRNA will be disrupted. Therefore, thermophiles must possess strategies to stabilize tRNA structures. To this end, several thermophile-specific modified nucleosides in tRNA have been identified. Other factors such as RNA-binding proteins and polyamines contribute to the stability of tRNA at high temperatures. Thermus thermophilus, which is an extreme-thermophilic eubacterium, can adapt its protein synthesis system in response to temperature changes via the network of modified nucleosides in tRNA and tRNA modification enzymes. Notably, tRNA modification enzymes from thermophiles are very stable. Therefore, they have been utilized for biochemical and structural studies. In the future, thermostable tRNA modification enzymes may be useful as biotechnology tools and may be utilized for medical science.

Effects of Polyamines on a Continuous Cell-Free Protein Synthesis System of an Extreme Thermophile, Thermus thermophilus

1993 ◽  
Vol 114 (5) ◽  
pp. 732-734 ◽  
Author(s):  
Taketoshi Uzawa ◽  
Akihiko Yamagishi ◽  
Takuya Ueda ◽  
Nobutoshi Chikazumi ◽  
Kimitsuna Watanabe ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Thermus Thermophilus ◽  
Extreme Thermophile ◽  
Synthesis System ◽  
Free Protein ◽  
Protein Synthesis System ◽  
Cell Free Protein Synthesis

scholarly journals Wobble tRNA modification and hydrophilic amino acid patterns dictate protein fate

2021 ◽  
Vol 12 (1) ◽  
Author(s):  
Francesca Rapino ◽  
Zhaoli Zhou ◽  
Ana Maria Roncero Sanchez ◽  
Marc Joiret ◽  
Christian Seca ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Expression ◽  
Protein Aggregation ◽  
Critical Role ◽  
Mrna Translation ◽  
Trna Modification ◽  
Translation Elongation ◽  
Hydrophilic Amino Acid ◽  
Protein Output

AbstractRegulation of mRNA translation elongation impacts nascent protein synthesis and integrity and plays a critical role in disease establishment. Here, we investigate features linking regulation of codon-dependent translation elongation to protein expression and homeostasis. Using knockdown models of enzymes that catalyze the mcm5s2 wobble uridine tRNA modification (U34-enzymes), we show that gene codon content is necessary but not sufficient to predict protein fate. While translation defects upon perturbation of U34-enzymes are strictly dependent on codon content, the consequences on protein output are determined by other features. Specific hydrophilic motifs cause protein aggregation and degradation upon codon-dependent translation elongation defects. Accordingly, the combination of codon content and the presence of hydrophilic motifs define the proteome whose maintenance relies on U34-tRNA modification. Together, these results uncover the mechanism linking wobble tRNA modification to mRNA translation and aggregation to maintain proteome homeostasis.

scholarly journals How Elongator Acetylates tRNA Bases

2020 ◽  
Vol 21 (21) ◽  
pp. 8209
Author(s):  
Nour-el-Hana Abbassi ◽  
Anna Biela ◽  
Sebastian Glatt ◽  
Ting-Yu Lin
Keyword(s):  
Protein Synthesis ◽  
Neurodegenerative Disorders ◽  
Trna Modification ◽  
Acetyl Coa ◽  
Translation Elongation ◽  
Transfer Rnas ◽  
Elongator Complex ◽  
Lysine Acetyltransferase ◽  
Ribosomal Translation

Elp3, the catalytic subunit of the eukaryotic Elongator complex, is a lysine acetyltransferase that acetylates the C5 position of wobble-base uridines (U34) in transfer RNAs (tRNAs). This Elongator-dependent RNA acetylation of anticodon bases affects the ribosomal translation elongation rates and directly links acetyl-CoA metabolism to both protein synthesis rates and the proteome integrity. Of note, several human diseases, including various cancers and neurodegenerative disorders, correlate with the dysregulation of Elongator’s tRNA modification activity. In this review, we focus on recent findings regarding the structure of Elp3 and the role of acetyl-CoA during its unique modification reaction.

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