Novel regulatory interactions and activities of mammalian tRNA synthetases

Young-Gyu Ko, Heonyong Park, Sunghoon Kim

Research output: Contribution to journalArticle

30 Citations (Scopus)

Abstract

Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids to their cognate tRNAs, thereby ensuring the faithful translation of genetic code. In addition to their enzymatic function, these enzymes have been discovered to regulate various cellular functions such as tRNA export, ribosomal RNA synthesis, apoptosis, inflammation and angiogenesis in mammalian. The insights into the noncanonical activities of these enzymes have been obtained from their unique cellular localization, interacting partners, isoform generation and expression control. Mammalian ARSs also form a macromolecular protein complex with a few auxiliary factors. Although the physiological significance of this complex is poorly understood, it also supports the potential of mammalian ARSs as sophisticated multifunctional proteins for regulating various cellular procedures. In this review, the novel regulatory activities of mammalian ARSs will be discussed in different biological processes.

Original languageEnglish
Pages (from-to)1304-1310
Number of pages7
JournalProteomics
Volume2
Issue number9
DOIs
Publication statusPublished - 2002 Sep 1
Externally publishedYes

Fingerprint

Amino Acyl-tRNA Synthetases
Transfer RNA
Genetic Code
Biological Phenomena
Multiprotein Complexes
Ribosomal RNA
Enzymes
Protein Isoforms
Apoptosis
Inflammation
Amino Acids
Proteins

Keywords

  • Aminoacyl-tRNA synthetase
  • Cellular localization
  • Noncanonical activities
  • Protein-protein interactions
  • Review

ASJC Scopus subject areas

  • Molecular Biology
  • Genetics

Cite this

Novel regulatory interactions and activities of mammalian tRNA synthetases. / Ko, Young-Gyu; Park, Heonyong; Kim, Sunghoon.

In: Proteomics, Vol. 2, No. 9, 01.09.2002, p. 1304-1310.

Research output: Contribution to journalArticle

Ko, Young-Gyu ; Park, Heonyong ; Kim, Sunghoon. / Novel regulatory interactions and activities of mammalian tRNA synthetases. In: Proteomics. 2002 ; Vol. 2, No. 9. pp. 1304-1310.
@article{9452c1053a8541d6905a840d56b32ad7,
title = "Novel regulatory interactions and activities of mammalian tRNA synthetases",
abstract = "Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids to their cognate tRNAs, thereby ensuring the faithful translation of genetic code. In addition to their enzymatic function, these enzymes have been discovered to regulate various cellular functions such as tRNA export, ribosomal RNA synthesis, apoptosis, inflammation and angiogenesis in mammalian. The insights into the noncanonical activities of these enzymes have been obtained from their unique cellular localization, interacting partners, isoform generation and expression control. Mammalian ARSs also form a macromolecular protein complex with a few auxiliary factors. Although the physiological significance of this complex is poorly understood, it also supports the potential of mammalian ARSs as sophisticated multifunctional proteins for regulating various cellular procedures. In this review, the novel regulatory activities of mammalian ARSs will be discussed in different biological processes.",
keywords = "Aminoacyl-tRNA synthetase, Cellular localization, Noncanonical activities, Protein-protein interactions, Review",
author = "Young-Gyu Ko and Heonyong Park and Sunghoon Kim",
year = "2002",
month = "9",
day = "1",
doi = "10.1002/1615-9861(200209)2:9<1304::AID-PROT1304>3.0.CO;2-E",
language = "English",
volume = "2",
pages = "1304--1310",
journal = "Proteomics",
issn = "1615-9853",
publisher = "Wiley-VCH Verlag",
number = "9",

}

TY - JOUR

T1 - Novel regulatory interactions and activities of mammalian tRNA synthetases

AU - Ko, Young-Gyu

AU - Park, Heonyong

AU - Kim, Sunghoon

PY - 2002/9/1

Y1 - 2002/9/1

N2 - Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids to their cognate tRNAs, thereby ensuring the faithful translation of genetic code. In addition to their enzymatic function, these enzymes have been discovered to regulate various cellular functions such as tRNA export, ribosomal RNA synthesis, apoptosis, inflammation and angiogenesis in mammalian. The insights into the noncanonical activities of these enzymes have been obtained from their unique cellular localization, interacting partners, isoform generation and expression control. Mammalian ARSs also form a macromolecular protein complex with a few auxiliary factors. Although the physiological significance of this complex is poorly understood, it also supports the potential of mammalian ARSs as sophisticated multifunctional proteins for regulating various cellular procedures. In this review, the novel regulatory activities of mammalian ARSs will be discussed in different biological processes.

AB - Aminoacyl-tRNA synthetases (ARSs) catalyze the attachment of specific amino acids to their cognate tRNAs, thereby ensuring the faithful translation of genetic code. In addition to their enzymatic function, these enzymes have been discovered to regulate various cellular functions such as tRNA export, ribosomal RNA synthesis, apoptosis, inflammation and angiogenesis in mammalian. The insights into the noncanonical activities of these enzymes have been obtained from their unique cellular localization, interacting partners, isoform generation and expression control. Mammalian ARSs also form a macromolecular protein complex with a few auxiliary factors. Although the physiological significance of this complex is poorly understood, it also supports the potential of mammalian ARSs as sophisticated multifunctional proteins for regulating various cellular procedures. In this review, the novel regulatory activities of mammalian ARSs will be discussed in different biological processes.

KW - Aminoacyl-tRNA synthetase

KW - Cellular localization

KW - Noncanonical activities

KW - Protein-protein interactions

KW - Review

UR - http://www.scopus.com/inward/record.url?scp=0036744432&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0036744432&partnerID=8YFLogxK

U2 - 10.1002/1615-9861(200209)2:9<1304::AID-PROT1304>3.0.CO;2-E

DO - 10.1002/1615-9861(200209)2:9<1304::AID-PROT1304>3.0.CO;2-E

M3 - Article

C2 - 12362348

AN - SCOPUS:0036744432

VL - 2

SP - 1304

EP - 1310

JO - Proteomics

JF - Proteomics

SN - 1615-9853

IS - 9

ER -