Hydrostatic pressure effects on several stages of protein synthesis in Escherichia coli

1974 ◽  
Vol 20 (3) ◽  
pp. 359-365 ◽  
Author(s):  
Michael J. Hardon ◽  
Lawrence J. Albright
Keyword(s):  
Escherichia Coli ◽  
Protein Synthesis ◽  
Hydrostatic Pressure ◽  
Specific Activity ◽  
Trna Synthetase ◽  
Pressure Effects ◽  
Acid Activation ◽  
Amino Acid Activation ◽  
The Stability ◽  
Translational Ambiguity

Hydrostatic pressure has been shown to inhibit protein synthesis in Escherichia coli by inhibiting amino acid activation and polypeptide synthesis in cell-free systems. Pressure may decrease translational ambiguity by suppressing any non-specific activity of phenylalanyl-tRNA synthetase and by preferentially decreasing the stability of leucyl-tRNA.

scholarly journals Asymmetric Amino Acid Activation by Class II Histidyl-tRNA Synthetase from Escherichia coli

2009 ◽  
Vol 284 (31) ◽  
pp. 20753-20762 ◽  
Author(s):  
Ethan Guth ◽  
Mindy Farris ◽  
Michael Bovee ◽  
Christopher S. Francklyn
Keyword(s):  
Escherichia Coli ◽  
Amino Acid ◽  
Class Ii ◽  
Trna Synthetase ◽  
Acid Activation ◽  
Amino Acid Activation

scholarly journals The mechanism of β-N-methylamino-l-alanine inhibition of tRNA aminoacylation and its impact on misincorporation

2019 ◽  
Vol 295 (5) ◽  
pp. 1402-1410 ◽  
Author(s):  
Nien-Ching Han ◽  
Tammy J. Bullwinkle ◽  
Kaeli F. Loeb ◽  
Kym F. Faull ◽  
Kyle Mohler ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Direct Evidence ◽  
Trna Synthetase ◽  
Acid Activation ◽  
Aminoacyl Trna Synthetase ◽  
Amino Acid Activation ◽  
Biochemical Assays ◽  
Serine Codons ◽  
Lateral Sclerosis

β-N-methylamino-l-alanine (BMAA) is a nonproteinogenic amino acid that has been associated with neurodegenerative diseases, including amyotrophic lateral sclerosis (ALS) and Alzheimer's disease (AD). BMAA has been found in human protein extracts; however, the mechanism by which it enters the proteome is still unclear. It has been suggested that BMAA is misincorporated at serine codons during protein synthesis, but direct evidence of its cotranslational incorporation is currently lacking. Here, using LC-MS–purified BMAA and several biochemical assays, we sought to determine whether any aminoacyl-tRNA synthetase (aaRS) utilizes BMAA as a substrate for aminoacylation. Despite BMAA's previously predicted misincorporation at serine codons, following a screen for amino acid activation in ATP/PPi exchange assays, we observed that BMAA is not a substrate for human seryl-tRNA synthetase (SerRS). Instead, we observed that BMAA is a substrate for human alanyl-tRNA synthetase (AlaRS) and can form BMAA-tRNAAla by escaping from the intrinsic AlaRS proofreading activity. Furthermore, we found that BMAA inhibits both the cognate amino acid activation and the editing functions of AlaRS. Our results reveal that, in addition to being misincorporated during translation, BMAA may be able to disrupt the integrity of protein synthesis through multiple different mechanisms.

scholarly journals Hydrostatic Pressure Effects on Protein Synthesis

1972 ◽  
Vol 12 (10) ◽  
pp. 1235-1250 ◽  
Author(s):  
C.E. Hildebrand ◽  
E.C. Pollard
Keyword(s):  
Protein Synthesis ◽  
Hydrostatic Pressure ◽  
Pressure Effects

Functional characterization of leucine-specific domain 1 from eukaryal and archaeal leucyl-tRNA synthetases

2010 ◽  
Vol 429 (3) ◽  
pp. 505-513 ◽  
Author(s):  
Xiao-Long Zhou ◽  
Meng Wang ◽  
Min Tan ◽  
Qian Huang ◽  
Gilbert Eriani ◽  
...  
Keyword(s):  
Functional Characterization ◽  
Trna Synthetase ◽  
Acid Activation ◽  
Reaction Step ◽  
Specific Domain ◽  
Binding Strength ◽  
Trna Synthetases ◽  
Amino Acid Activation ◽  
Common Domain

LeuRS (leucyl-tRNA synthetase) catalyses the esterification of tRNAsLeu with leucine. This family of enzymes is divided into prokaryotic and eukaryal/archaeal groups according to the presence and position of specific insertions and extensions. In the present study, we investigated the function of LSD1 (leucine-specific domain 1), which is naturally present in eukaryal/archaeal LeuRSs, but absent from prokaryotic LeuRSs. When mutated in their common domain, the eukaryal and archaeal LeuRSs exhibited defects in the first reaction step of amino acid activation with variations of leucine or ATP-binding strength, whereas the tRNA aminoacylation was moderately affected. When the eukaryal extension was mutated, severe tRNA charging defects were observed, suggesting that eukaryotes evolved this LSD1 extension in order to improve the aminoacylation reaction step. The results also showed that the LSD1s from organisms of both groups are dispensable for post-transfer editing. Together, the data provide us with a further understanding of the organization and structure of LeuRS domains.

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