2015
DOI: 10.1074/jbc.m115.690867
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Assembly of Multi-tRNA Synthetase Complex via Heterotetrameric Glutathione Transferase-homology Domains

Abstract: Background: GST domains have been found in diverse proteins involved in translational systems. Results: Four GST domains from human methionyl-tRNA synthetase, glutaminyl-prolyl-tRNA synthetase, ARS-interacting multifunctional protein (AIMP) 2, and AIMP3 are complexed in an ordered fashion. Conclusion: Four components in the human multisynthetase complex are assembled through a GST domain tetrameric complex. Significance: GST domain assemblies act as scaffolds for the formation of multicomponent protein complex… Show more

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Cited by 62 publications
(91 citation statements)
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“…Bifunctional EPRS exists in dimeric form (mediated by antiparallel dimerization of the carboxy-terminal PRS domain) 32 and resides at the exterior of the MSC 4,9,11,12 . Size-exclusion chromatography revealed that the amino-terminal GST and ERS domains were not involved in the dimerization (data not shown).…”
Section: Discussionmentioning
confidence: 99%
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“…Bifunctional EPRS exists in dimeric form (mediated by antiparallel dimerization of the carboxy-terminal PRS domain) 32 and resides at the exterior of the MSC 4,9,11,12 . Size-exclusion chromatography revealed that the amino-terminal GST and ERS domains were not involved in the dimerization (data not shown).…”
Section: Discussionmentioning
confidence: 99%
“…Size-exclusion chromatography revealed that the amino-terminal GST and ERS domains were not involved in the dimerization (data not shown). This unique dimeric conformation of EPRS might be important for maintaining the integrity of the MSC, as both amino-terminal GST-like domains interact with the respective GST-like domains in the dimeric AIMP2 molecule (core scaffold protein of MSC) 11 . The central WHEP domains located between the ERS and PRS domains might have a role in associating the catalytic domains with the MSC.…”
Section: Discussionmentioning
confidence: 99%
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“…The next part (46-114) contains a heptad repeat region (L52-I80) forming a coiled-coil structure for the interaction to AIMP1 (26). The remaining part of AIMP2 (115-320) forms a GST domain, the structure of which was determined as a complex with the GST domain of EPRS (1-175), which is one of the interacting partners in the MSC (27). In the crystal structure (PDB 5A34), GST domains of AIMP2 and EPRS form a canonical GST dimer (Fig.…”
Section: Structural Analysis Of Aimp2 For Nuclear Translocation and Mmentioning
confidence: 99%
“…As AIMP1 is anchored to AIMP2 via coiled-coil interaction of leucine zipper (26), RRS and QRS may be located proximal to AIMP2. MRS and AIMP3 are also linked to AIMP2 via EPRS through the tetrameric complex of their GST domains (27). Another critical region in AIMP2 is 193-203 for DRS binding (13), and it is around b4 strand in GST-N, being located near S156.…”
Section: Structural Analysis Of Aimp2 For Nuclear Translocation and Mmentioning
confidence: 99%