scholarly journals The role of nucleotides in position 1 and 72 of the tRNATyr acceptor stem in aminoacylation by bovine tyrosyl-tRNA synthetase

2002 ◽  
Vol 18 (1) ◽  
pp. 71-75
Author(s):  
V. G. Naidenov ◽  
M. I. Vudmaska ◽  
G. Kh. Matsuka
Keyword(s):  
Trna Synthetase ◽  
Acceptor Stem

Critical Role of the Acceptor Stem of tRNAsMet in their Aminoacylation by Escherichia coli Methionyl-tRNA Synthetase

1993 ◽  
Vol 229 (1) ◽  
pp. 26-36 ◽  
Author(s):  
Thierry Meinnel ◽  
Yves Mechulam ◽  
Christine Lazennec ◽  
Sylvain Blanquet ◽  
Guy Fayat
Keyword(s):  
Escherichia Coli ◽  
Critical Role ◽  
Trna Synthetase ◽  
Acceptor Stem ◽  
Methionyl Trna Synthetase

scholarly journals Role of the CCA terminal sequence of tRNA(Val) in aminoacylation with valyl-tRNA synthetase.

1994 ◽  
Vol 269 (35) ◽  
pp. 22173-22177 ◽  
Author(s):  
K. Tamura ◽  
N. Nameki ◽  
T. Hasegawa ◽  
M. Shimizu ◽  
H. Himeno
Keyword(s):  
Trna Synthetase ◽  
Terminal Sequence

scholarly journals Advances in the Role of Leucine-Sensing in the Regulation of Protein Synthesis in Aging Skeletal Muscle

2021 ◽  
Vol 9 ◽  
Author(s):  
Yan Zhao ◽  
Jason Cholewa ◽  
Huayu Shang ◽  
Yueqin Yang ◽  
Xiaomin Ding ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Therapeutic Potential ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Trna Synthetase ◽  
Limiting Factor ◽  
Anabolic Resistance ◽  
Age Related

Skeletal muscle anabolic resistance (i.e., the decrease in muscle protein synthesis (MPS) in response to anabolic stimuli such as amino acids and exercise) has been identified as a major cause of age-related sarcopenia, to which blunted nutrition-sensing contributes. In recent years, it has been suggested that a leucine sensor may function as a rate-limiting factor in skeletal MPS via small-molecule GTPase. Leucine-sensing and response may therefore have important therapeutic potential in the steady regulation of protein metabolism in aging skeletal muscle. This paper systematically summarizes the three critical processes involved in the leucine-sensing and response process: (1) How the coincidence detector mammalian target of rapamycin complex 1 localizes on the surface of lysosome and how its crucial upstream regulators Rheb and RagB/RagD interact to modulate the leucine response; (2) how complexes such as Ragulator, GATOR, FLCN, and TSC control the nucleotide loading state of Rheb and RagB/RagD to modulate their functional activity; and (3) how the identified leucine sensor leucyl-tRNA synthetase (LARS) and stress response protein 2 (Sestrin2) participate in the leucine-sensing process and the activation of RagB/RagD. Finally, we discuss the potential mechanistic role of exercise and its interactions with leucine-sensing and anabolic responses.

scholarly journals Functional role of C-terminal domain of Thermus thermophilus leucyl-tRNA synthetase

2010 ◽  
Vol 26 (6) ◽  
pp. 478-485 ◽  
Author(s):  
O. I. Gudzera ◽  
A. D. Yaremchuk ◽  
M. A. Tukalo
Keyword(s):  
Functional Role ◽  
Thermus Thermophilus ◽  
Trna Synthetase ◽  
Terminal Domain

scholarly journals Functional genetic encoding of sulfotyrosine in mammalian cells

2020 ◽  
Vol 11 (1) ◽  
Author(s):  
Xinyuan He ◽  
Yan Chen ◽  
Daisy Guiza Beltran ◽  
Maia Kelly ◽  
Bin Ma ◽  
...  
Keyword(s):  
Mammalian Cells ◽  
Biochemical Characterization ◽  
Trna Synthetase ◽  
Functional Verification ◽  
Cellular Processes ◽  
Genetic Encoding ◽  
Efficient Expression

Abstract Protein tyrosine O-sulfation (PTS) plays a crucial role in extracellular biomolecular interactions that dictate various cellular processes. It also involves in the development of many human diseases. Regardless of recent progress, our current understanding of PTS is still in its infancy. To promote and facilitate relevant studies, a generally applicable method is needed to enable efficient expression of sulfoproteins with defined sulfation sites in live mammalian cells. Here we report the engineering, in vitro biochemical characterization, structural study, and in vivo functional verification of a tyrosyl-tRNA synthetase mutant for the genetic encoding of sulfotyrosine in mammalian cells. We further apply this chemical biology tool to cell-based studies on the role of a sulfation site in the activation of chemokine receptor CXCR4 by its ligand. Our work will not only facilitate cellular studies of PTS, but also paves the way for economical production of sulfated proteins as therapeutic agents in mammalian systems.

The Seryl-tRNA synthetase/tRNASer acceptor stem interface is mediated via a specific network of water molecules

2011 ◽  
Vol 412 (4) ◽  
pp. 532-536 ◽  
Author(s):  
André Eichert ◽  
Dominik Oberthuer ◽  
Christian Betzel ◽  
Reinhard Geßner ◽  
Volker A. Erdmann ◽  
...  
Keyword(s):  
Trna Synthetase ◽  
Water Molecules ◽  
Acceptor Stem

Anticodon and acceptor stem nucleotides in tRNAGln are major recognition elements for E. coli glutaminyl-tRNA synthetase

Nature ◽  
1991 ◽  
Vol 352 (6332) ◽  
pp. 258-260 ◽  
Author(s):  
Martina Jahn ◽  
M. John Rogers ◽  
Dieter Söll
Keyword(s):  
Trna Synthetase ◽  
E Coli ◽  
Acceptor Stem ◽  
Recognition Elements

Glucose-dependent control of leucine metabolism by leucyl-tRNA synthetase 1

Science ◽  
2019 ◽  
pp. eaau2753 ◽  
Author(s):  
Ina Yoon ◽  
Miso Nam ◽  
Hoi Kyoung Kim ◽  
Hee-Sun Moon ◽  
Sungmin Kim ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Energy Production ◽  
Trna Synthetase ◽  
Glucose Starvation ◽  
Catabolic Pathway ◽  
Inhibit Protein Synthesis ◽  
Support Cell ◽  
Save Energy

Despite the importance of glucose and amino acids for energy metabolism, interactions between the two nutrients are not well understood. We provide evidence for a role of leucyl-tRNA synthetase 1 (LARS1) in glucose-dependent control of leucine usage. Upon glucose starvation, LARS1 was phosphorylated by Unc-51 like autophagy activating kinase 1 (ULK1) at the residues crucial for leucine-binding. The phosphorylated LARS1 showed decreased leucine-binding, which may inhibit protein synthesis and help save energy. Leucine, not used to anabolic process, may be available to catabolic pathway for energy generation. The LARS1-mediated changes in leucine utilization might help support cell survival deprived of glucose. Thus, dependent on the availability of glucose, LARS1 may help regulate whether leucine is used for protein synthesis or energy production.

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