Interactions of aminoacyl-tRNA synthetases in high-molecular-weight multienzyme complexes from rat liver

Dang, Chi V.; Ferguson, B; Burke, D.; Garcia, V.; Yang, David C.H.

doi:10.1016/0167-4838(85)90239-0

Cited by 20 publications

(6 citation statements)

References 23 publications

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“…First, aminoacylation activities of mammalian LysRS are similar whether bound in the MSC or free of the complex ( e.g. , after high salt treatment) (Dang et al, 1985; Mirande et al, 1983), indicating that the architecture of the MSC is compatible with aminoacylation activities. Accordingly, the reconstituted LysRS-p38/AIMP2 sub-complexes are fully functional for aminoacylation (Fang et al, 2011).…”

Section: Resultsmentioning

confidence: 99%

Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription

Ofir-Birin¹,

et al. 2013

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SUMMARY Lysyl-tRNA synthetase (LysRS), a component of the translation apparatus, is released from the cytoplasmic multi-tRNA synthetase complex (MSC) to activate the transcription factor MITF in stimulated mast cells through undefined mechanisms. Here we show that Ser207-phosphorylation provokes a new conformer of LysRS that inactivates its translational, but activates its transcriptional function. The crystal structure of an MSC sub-complex established that LysRS is held in the MSC by binding to the N-terminus of the scaffold protein p38/AIMP2. Phosphorylation-created steric clashes at the LysRS domain interface disrupt its binding grooves for p38/AIMP2, releasing LysRS and provoking its nuclear translocation. This alteration also exposes the C-terminal domain of LysRS to bind to MITF and triggers LysRS-directed production of the second messenger Ap4A that activates MITF. Thus our results establish that a single conformational change triggered by phosphorylation leads to multiple effects driving an exclusive switch of LysRS function from translation to transcription.

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Section: Resultsmentioning

confidence: 99%

Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription

Ofir-Birin¹,

et al. 2013

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“…The complexed and free aminoacyl-tRNA synthetases appeared to have similar substrate affinities as determined by steady-state kinetics in most instances (Dang et al, 1985;Mirande et al, 1983a;Vellekamp et al, 1985). Simultaneous aminoacylation reactions catalysed by the complex occurred independently (Dang et al, 1985;Mirande et al, 1983a). The aminoacyl-tRNA synthetase multienzyme complex is unique in that it catalyses parallel reactions that do not appear to affect each other.…”

Section: Functional Significance Of Aminoacyl-trna Synthetase Complexmentioning

confidence: 88%

Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic

Dang¹

1986

Biochemical Journal

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“…Aminoacyl-tRNA synthetases, the family of enzymes which aminacylate tRNA molecules, were first observed in the 1980s to form high molecular weight complexes of then-unknown function [44]. The multisynthetase complexes appear to play multiple roles depending on cellular conditions and since their original discovery have been associated with several processes from substrate channeling in protein biosynthesis to cytokine release in the inflammation response [45].…”

Section: A J Wirth and M Gruebelementioning

confidence: 99%

Quinary protein structure and the consequences of crowding in living cells: Leaving the test‐tube behind

2013

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Although the importance of weak protein-protein interactions has been understood since the 1980s, scant attention has been paid to this "quinary structure". The transient nature of quinary structure facilitates dynamic sub-cellular organization through loose grouping of proteins with multiple binding partners. Despite our growing appreciation of the quinary structure paradigm in cell biology, we do not yet understand how the many forces inside the cell--the excluded volume effect, the "stickiness" of the cytoplasm, and hydrodynamic interactions--perturb the weakest functional protein interactions. We discuss the unresolved problem of how the forces in the cell modulate quinary structure, and to what extent the cell has evolved to exert control over the weakest biomolecular interactions. We conclude by highlighting the new experimental and computational tools coming on-line for in vivo studies, which are a critical next step if we are to understand quinary structure in its native environment.

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Interactions of aminoacyl-tRNA synthetases in high-molecular-weight multienzyme complexes from rat liver

Cited by 20 publications

References 23 publications

Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription

Structural Switch of Lysyl-tRNA Synthetase between Translation and Transcription

Multienzyme complex of aminoacyl-tRNA synthetases: an essence of being eukaryotic

Quinary protein structure and the consequences of crowding in living cells: Leaving the test‐tube behind

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