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Last update 08 May 2025

TrpRS

Last update 08 May 2025

Basic Info

Synonyms

hWRS, IFI53, IFP53

+ [10]

Introduction

Has no angiostatic activity. Possesses an angiostatic activity but has no aminoacylation activity (PubMed:11773625, PubMed:11773626, PubMed:14630953). Inhibits fluid shear stress-activated responses of endothelial cells (PubMed:14630953). Regulates ERK, Akt, and eNOS activation pathways that are associated with angiogenesis, cytoskeletal reorganization and shear stress-responsive gene expression (PubMed:14630953). Has an angiostatic activity. Catalyzes the attachment of tryptophan to tRNA(Trp) in a two-step reaction: tryptophan is first activated by ATP to form Trp-AMP and then transferred to the acceptor end of the tRNA(Trp).

Drugs associated with TrpRS

Chuangxinmycin

Target

TrpRS

Mechanism

TrpRS inhibitors

Active Org.

Shandong University

Originator Org.

Shandong University

Active Indication

Bacterial Infections

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

M-101AI

Target

TrpRS

Mechanism

TrpRS inhibitors

Active Org.

MirimGENE Co. Ltd.

Originator Org.

MirimGENE Co. Ltd.

Active Indication

Sepsis

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

M-207AN

Target

TrpRS

Mechanism

TrpRS inhibitors

Active Org.

MirimGENE Co. Ltd.

Originator Org.

MirimGENE Co. Ltd.

Active Indication

Tuberculosis

Inactive Indication-

Drug Highest PhasePreclinical

First Approval Ctry. / Loc.-

First Approval Date20 Jan 1800

100 Clinical Results associated with TrpRS

100 Translational Medicine associated with TrpRS

0 Patents (Medical) associated with TrpRS

377

Literatures (Medical) associated with TrpRS

01 Apr 2025·Acta Crystallographica Section F Structural Biology Communications

The crystal structures of apo and tryptophan-bound tryptophanyl-tRNA synthetase from Neisseria gonorrhoeae

Article

Author: Staker, Bart L ; Dranow, David M ; Baral, Jessika ; Myler, Peter ; Lorimer, Donald D ; Song, David ; Edwards, Thomas E ; Smith, Craig L

Neisseria gonorrhoeae, the causative agent of the human disease gonorrhea, is the second most common sexually transmitted pathogen in the United States. Gonorrhea has a significantly high morbidity rate due to the ability of N. gonorrhoeae to rapidly develop antibiotic resistance. In this paper, crystal structures of tryptophanyl-tRNA synthetase (TrpRS) from N. gonorrhoeae (NgTrpRS) were determined in both its apo form and in complex with tryptophan. The structures reveal conserved HIGH and KMSKS motifs critical for ATP binding and catalysis, and highlight conformational changes in the active site upon tryptophan binding, including a methionine flip and the rearrangement of hydrogen-bonding residues. Structural alignments with human TrpRS isoforms demonstrate significant differences between the bacterial and human cytosolic forms, particularly in their active sites. While NgTrpRS and human mitochondrial TrpRS share conserved catalytic residues that are essential for binding tryptophan and indolmycin, the cytosolic TrpRS contains substitutions that introduce steric hindrance, limiting the binding of indolmycin. These results provide insight for the development of inhibitors targeting bacterial TrpRS without affecting the human mitochondrial or cytosolic isoforms, contributing to efforts to combat antibiotic-resistant N. gonorrhoeae infections.

01 Mar 2025·Nature Genetics

The contribution of genetic determinants of blood gene expression and splicing to molecular phenotypes and health outcomes

Article

Author: Burnham, Katie L ; Tokolyi, Alex ; Thurston, Scott A J ; Roberts, David J ; Iyer, Vivek ; Persyn, Elodie ; Tardaguila, Manuel ; Whelan, Christopher D ; Gaffney, Daniel J ; Noell, Guillaume ; Runz, Heiko ; Peters, James E ; Davenport, Emma E ; Nath, Artika P ; Quail, Michael A ; Marten, Jonathan ; Paul, Dirk S ; Farr, Ben ; Stacey, David ; Soranzo, Nicole ; Inouye, Michael ; Danesh, John ; Ritchie, Scott C ; Vanderstichele, Thomas ; Di Angelantonio, Emanuele ; Lambert, Samuel A ; Xu, Yu ; Petrovski, Slavé ; Butterworth, Adam S ; Jiang, Xilin ; Rajan, Diana ; Sun, Benjamin B

AbstractThe biological mechanisms through which most nonprotein-coding genetic variants affect disease risk are unknown. To investigate gene-regulatory mechanisms, we mapped blood gene expression and splicing quantitative trait loci (QTLs) through bulk RNA sequencing in 4,732 participants and integrated protein, metabolite and lipid data from the same individuals. We identified cis-QTLs for the expression of 17,233 genes and 29,514 splicing events (in 6,853 genes). Colocalization analyses revealed 3,430 proteomic and metabolomic traits with a shared association signal with either gene expression or splicing. We quantified the relative contribution of the genetic effects at loci with shared etiology, observing 222 molecular phenotypes significantly mediated by gene expression or splicing. We uncovered gene-regulatory mechanisms at disease loci with therapeutic implications, such as WARS1 in hypertension, IL7R in dermatitis and IFNAR2 in COVID-19. Our study provides an open-access resource on the shared genetic etiology across transcriptional phenotypes, molecular traits and health outcomes in humans (https://IntervalRNA.org.uk).

01 Jan 2025·Metabolism

Wars1 downregulation in hepatocytes induces mitochondrial stress and disrupts metabolic homeostasis

Article

Author: Benegiamo, Giorgia ; Demagny, Hadrien ; Faure, Adrien ; Perino, Alessia ; Auwerx, Johan ; Schoonjans, Kristina ; Li, Xiaoxu ; Jalil, Antoine ; Pontanari, Francesca

Several laboratories, including ours, have employed the Slc25a47^{tm1c(EUCOMM)Hmgu} mouse model to investigate the role of SLC25A47, a hepatocyte-specific mitochondrial carrier, in regulating hepatic metabolism and systemic physiology. In this study, we reveal that the hepatic and systemic phenotypes observed following recombination of the Slc25a47-Wars1 locus in hepatocytes are primarily driven by the unexpected downregulation of Wars1, the cytosolic tryptophan aminoacyl-tRNA synthetase located adjacent to Slc25a47. While the downregulation of Wars1 predictably affects cytosolic translation, we also observed a significant impairment in mitochondrial protein synthesis within hepatocytes. This disturbance in mitochondrial function leads to an activation of the mitochondrial unfolded protein response (UPR^mt), a critical component of the mitochondrial stress response (MSR). Our findings clarify the distinct roles of Slc25a47 and Wars1 in maintaining both systemic and hepatic metabolic homeostasis. This study sheds new light on the broader implications of aminoacyl-tRNA synthetases in mitochondrial physiology and stress responses.

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TrpRS

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