Evolution of the multi-tRNA synthetase complex and its role in cancer
© 2019 Hyeon et al..
Aminoacyl-tRNA synthetases (ARSs) are enzymes that ligate their cognate amino acids to tRNAs for protein synthesis. However, recent studies have shown that their functions are expanded beyond protein synthesis through the interactions with diverse cellular factors. In this review, we discuss how ARSs have evolved to expand and control their functions by forming protein assemblies. We particularly focus on a macromolecular ARS complex in eukaryotes, named multi-tRNA synthetase complex (MSC), which is proposed to provide a channel through which tRNAs reach bound ARSs to receive their cognate amino acid and transit further to the translation machinery. Approximately half of the ARSs assemble into the MSC through cis-acting noncatalytic domains attached to their catalytic domains and trans-acting factors. Evolution of the MSC included its functional expansion, during which the MSC interaction network was augmented by additional cellular pathways present in higher eukaryotes. We also discuss MSC components that could be functionally involved in the pathophysiology of tumorigenesis. For example, the activities of some trans-acting factors have tumor-suppressing effects or maintain DNA integrity and are functionally compromised in cancer. On the basis of Gene Ontology analyses, we propose that the regulatory activities of the MSC-associated ARSs mainly converge on five biological processes, including mammalian target of rapamycin (mTOR) and DNA repair pathways. Future studies are needed to investigate how the MSC-associated and free-ARSs interact with each other and other factors in the control of multiple cellular pathways, and how aberrant or disrupted interactions in the MSC can cause disease.
| Medienart: |
E-Artikel |
|---|
| Erscheinungsjahr: |
2019 |
|---|---|
| Erschienen: |
2019 |
| Enthalten in: |
Zur Gesamtaufnahme - volume:294 |
|---|---|
| Enthalten in: |
The Journal of biological chemistry - 294(2019), 14 vom: 05. Apr., Seite 5340-5351 |
| Sprache: |
Englisch |
|---|
| Beteiligte Personen: |
Hyeon, Do Young [VerfasserIn] |
|---|
| Links: |
|---|
| Anmerkungen: |
Date Completed 16.10.2019 Date Revised 11.10.2023 published: Print-Electronic Citation Status MEDLINE |
|---|
| doi: |
10.1074/jbc.REV118.002958 |
|---|
| funding: |
|
|---|---|
| Förderinstitution / Projekttitel: |
|
| PPN (Katalog-ID): |
NLM294080619 |
|---|
| LEADER | 01000naa a22002652 4500 | ||
|---|---|---|---|
| 001 | NLM294080619 | ||
| 003 | DE-627 | ||
| 005 | 20231225080723.0 | ||
| 007 | cr uuu---uuuuu | ||
| 008 | 231225s2019 xx |||||o 00| ||eng c | ||
| 024 | 7 | |a 10.1074/jbc.REV118.002958 |2 doi | |
| 028 | 5 | 2 | |a pubmed24n0980.xml |
| 035 | |a (DE-627)NLM294080619 | ||
| 035 | |a (NLM)30782841 | ||
| 040 | |a DE-627 |b ger |c DE-627 |e rakwb | ||
| 041 | |a eng | ||
| 100 | 1 | |a Hyeon, Do Young |e verfasserin |4 aut | |
| 245 | 1 | 0 | |a Evolution of the multi-tRNA synthetase complex and its role in cancer |
| 264 | 1 | |c 2019 | |
| 336 | |a Text |b txt |2 rdacontent | ||
| 337 | |a ƒaComputermedien |b c |2 rdamedia | ||
| 338 | |a ƒa Online-Ressource |b cr |2 rdacarrier | ||
| 500 | |a Date Completed 16.10.2019 | ||
| 500 | |a Date Revised 11.10.2023 | ||
| 500 | |a published: Print-Electronic | ||
| 500 | |a Citation Status MEDLINE | ||
| 520 | |a © 2019 Hyeon et al. | ||
| 520 | |a Aminoacyl-tRNA synthetases (ARSs) are enzymes that ligate their cognate amino acids to tRNAs for protein synthesis. However, recent studies have shown that their functions are expanded beyond protein synthesis through the interactions with diverse cellular factors. In this review, we discuss how ARSs have evolved to expand and control their functions by forming protein assemblies. We particularly focus on a macromolecular ARS complex in eukaryotes, named multi-tRNA synthetase complex (MSC), which is proposed to provide a channel through which tRNAs reach bound ARSs to receive their cognate amino acid and transit further to the translation machinery. Approximately half of the ARSs assemble into the MSC through cis-acting noncatalytic domains attached to their catalytic domains and trans-acting factors. Evolution of the MSC included its functional expansion, during which the MSC interaction network was augmented by additional cellular pathways present in higher eukaryotes. We also discuss MSC components that could be functionally involved in the pathophysiology of tumorigenesis. For example, the activities of some trans-acting factors have tumor-suppressing effects or maintain DNA integrity and are functionally compromised in cancer. On the basis of Gene Ontology analyses, we propose that the regulatory activities of the MSC-associated ARSs mainly converge on five biological processes, including mammalian target of rapamycin (mTOR) and DNA repair pathways. Future studies are needed to investigate how the MSC-associated and free-ARSs interact with each other and other factors in the control of multiple cellular pathways, and how aberrant or disrupted interactions in the MSC can cause disease | ||
| 650 | 4 | |a Journal Article | |
| 650 | 4 | |a Research Support, Non-U.S. Gov't | |
| 650 | 4 | |a Review | |
| 650 | 4 | |a Aminoacyl-tRNA synthetases | |
| 650 | 4 | |a Cancer | |
| 650 | 4 | |a aminoacyl tRNA synthetase | |
| 650 | 4 | |a cancer biology | |
| 650 | 4 | |a intracellular processing | |
| 650 | 4 | |a multi-tRNA synthetase complex | |
| 650 | 4 | |a network analysis | |
| 650 | 4 | |a pathology | |
| 650 | 4 | |a protein synthesis | |
| 650 | 4 | |a protein–protein interaction | |
| 650 | 7 | |a Multienzyme Complexes |2 NLM | |
| 650 | 7 | |a Neoplasm Proteins |2 NLM | |
| 650 | 7 | |a MTOR protein, human |2 NLM | |
| 650 | 7 | |a EC 2.7.1.1 |2 NLM | |
| 650 | 7 | |a TOR Serine-Threonine Kinases |2 NLM | |
| 650 | 7 | |a EC 2.7.11.1 |2 NLM | |
| 650 | 7 | |a Amino Acyl-tRNA Synthetases |2 NLM | |
| 650 | 7 | |a EC 6.1.1.- |2 NLM | |
| 700 | 1 | |a Kim, Jong Hyun |e verfasserin |4 aut | |
| 700 | 1 | |a Ahn, Tae Jin |e verfasserin |4 aut | |
| 700 | 1 | |a Cho, Yeshin |e verfasserin |4 aut | |
| 700 | 1 | |a Hwang, Daehee |e verfasserin |4 aut | |
| 700 | 1 | |a Kim, Sunghoon |e verfasserin |4 aut | |
| 773 | 0 | 8 | |i Enthalten in |t The Journal of biological chemistry |d 1945 |g 294(2019), 14 vom: 05. Apr., Seite 5340-5351 |w (DE-627)NLM000004995 |x 1083-351X |7 nnns |
| 773 | 1 | 8 | |g volume:294 |g year:2019 |g number:14 |g day:05 |g month:04 |g pages:5340-5351 |
| 856 | 4 | 0 | |u http://dx.doi.org/10.1074/jbc.REV118.002958 |3 Volltext |
| 912 | |a GBV_USEFLAG_A | ||
| 912 | |a GBV_NLM | ||
| 951 | |a AR | ||
| 952 | |d 294 |j 2019 |e 14 |b 05 |c 04 |h 5340-5351 | ||