Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases

Jeongwoo Kang, Taeho Kim, Young-Gyu Ko, Seung Bae Rho, Sang Gyu Park, Min Jung Kim, Ho Jeong Kwon, Sunghoon Kim

Research output: Contribution to journalArticle

27 Citations (Scopus)

Abstract

Heat shock protein 90 (hsp90) is a molecular chaperone responsible for protein folding and maturation in vivo. Interaction of hsp90 with human glutamyl-prolyl-tRNA synthetase (EPRS) was found by genetic screening, co-immunoprecipitation, and in vitro binding experiments. This interaction was sensitive to the hsp90 inhibitor, geldanamycin, and also ATP, suggesting thai the chaperone activity of hsp90 is required for interaction with EPRS. Interaction of EPRS with hsp90 was targeted to the region of three tandem repeats linking the two catalytic domains of EPRS that is also responsible for the interaction with isoleucyl-tRNA synthetase (IRS). Interaction of EPRS and IRS also depended on the activity of hsp90, implying that their association was mediated by hsp90. EPRS and IRS form a macromolecular protein complex with at least six other tRNA synthetases and three cofactors, hsp90 preferentially binds to most of the complex-forming enzymes rather than those that are not found in the complex. In addition, inactivation of hsp90 interfered with the in vivo incorporation of the nascent aminoacyl-tRNA synthetases into the multi-ARS complex. Thus, hsp90 appears to mediate protein-protein interactions of mammalian tRNA synthetases.

Original languageEnglish
Pages (from-to)31682-31688
Number of pages7
JournalJournal of Biological Chemistry
Volume275
Issue number41
Publication statusPublished - 2000 Oct 13
Externally publishedYes

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HSP90 Heat-Shock Proteins
Amino Acyl-tRNA Synthetases
Isoleucine-tRNA Ligase
Proteins
Protein folding
Multiprotein Complexes
Tandem Repeat Sequences
Molecular Chaperones
Protein Folding
Genetic Testing
Immunoprecipitation
Catalytic Domain
Screening
Adenosine Triphosphate
Association reactions

ASJC Scopus subject areas

  • Biochemistry

Cite this

Kang, J., Kim, T., Ko, Y-G., Rho, S. B., Park, S. G., Kim, M. J., ... Kim, S. (2000). Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. Journal of Biological Chemistry, 275(41), 31682-31688.

Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. / Kang, Jeongwoo; Kim, Taeho; Ko, Young-Gyu; Rho, Seung Bae; Park, Sang Gyu; Kim, Min Jung; Kwon, Ho Jeong; Kim, Sunghoon.

In: Journal of Biological Chemistry, Vol. 275, No. 41, 13.10.2000, p. 31682-31688.

Research output: Contribution to journalArticle

Kang, J, Kim, T, Ko, Y-G, Rho, SB, Park, SG, Kim, MJ, Kwon, HJ & Kim, S 2000, 'Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases', Journal of Biological Chemistry, vol. 275, no. 41, pp. 31682-31688.
Kang, Jeongwoo ; Kim, Taeho ; Ko, Young-Gyu ; Rho, Seung Bae ; Park, Sang Gyu ; Kim, Min Jung ; Kwon, Ho Jeong ; Kim, Sunghoon. / Heat shock protein 90 mediates protein-protein interactions between human aminoacyl-tRNA synthetases. In: Journal of Biological Chemistry. 2000 ; Vol. 275, No. 41. pp. 31682-31688.
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