Mammalian high-molecular-weight and monomeric forms of valyl-tRNA synthetase

Godar, Dianne E.; Yang, David C.H.

doi:10.1021/bi00406a055

Cited by 12 publications

(5 citation statements)

References 35 publications

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“…Interestingly the N-terminal region of EF-1 resembles somewhat the N-terminal region of certain amino-acyl-tRNA synthetases (5) and one of the eucaryotic synthetases, valyl-tRNA-synthetase, is described to form a complex with a heavy molecular weight form of EF-1 (6,7). The high molecular weight form of the synthetase reportedly dissociates when its EF-ly related N-terminus is removed by protease (8). Another hint for a new role of EF-l1y, namely the control of translation originates from Lew et al who show that EF-l-y is highly overexpressed in certain colon and pancreas carcinomas (9).…”

Section: Introductionmentioning

confidence: 99%

Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation

1992

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Copy-DNA clones covering the complete coding sequence of human Elongation Factor-1 gamma mRNA have been isolated and characterized. The expression of Elongation Factor-1 in a variety of cell lines and a number of tissues shows a large increase in Elongation Factor-1 mRNA going from tissue to cultured cells (20-fold). Messenger-RNA levels for Elongation Factor-1 alpha, -1 beta and -1 gamma increase in parallel suggesting coordinate regulation of the expression of these genes. Oncogenic transformation in vitro does not strongly affect Elongation Factor-1 mRNA levels.

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Section: Introductionmentioning

confidence: 99%

Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation

1992

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“…Proteolytic degradation may be the reason for the failure of early attempts to isolate the complex. Using phenylmethylsulphonyl fluoride only, Yang et al [22] reported the purification of fully active free ValtRNA synthetase with a molecular mass of about 140 kDa. The active 116-kDa polypeptide was also isolated in our laboratory (data not shown).…”

Section: Discussionmentioning

confidence: 99%

“…Bars indicate sample standard deviation et al [22], that the complex has the shape of a prolonged ellipsoid with a ratio of axes of 6.5, the molecular mass obtained by gel filtration may be overestimated. Thus, it seems most probable that the complex contains two sets of subunits and has a molecular mass about 620 kDa.…”

Section: Without Ef-i ( a ) Amounts Of Protcin Equivalent To I Prnomentioning

confidence: 99%

Purification and properties of a high‐molecular‐mass complex between Val‐tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells

Motorin

Wolfson

Löhr

et al. 1991

European Journal of Biochemistry

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In extracts of various mammalian tissues obtained in the presence of protease inhibitors Val‐tRNA synthetase exists exclusively as a complex with a molecular mass of about 800 kDa. This complex was purified by gel filtration and two HPLC steps and contained five different polypeptides with molecular masses of 140, 50, 50, 40 and 30 kDa. The complex seems to have no tissue or species specificity, because preparations with identical polypeptide composition were obtained by the same method from rabbit liver and reticulocytes, and rat and beef liver. Four low‐molecular‐mass polypeptides were identified by two‐dimensional electrophoresis as subunits of the heavy form of elongation factor 1 (EF‐1H). The complex possesses the activity of EF‐1 in the poly(U)‐directed translation system, indicating that EF‐1H is an integral part of the complex. Gel filtration of the tissue extracts reveals three different peaks of EF‐1 activity, corresponding to EF‐1α, EF‐1H and the high‐molecular‐mass complex of Val‐tRNA synthetase and EF‐1H. All activity of Val‐tRNA synthetase and about 25% of EF‐1 activity are associated with the complex. Different forms of EF‐1 revealed no significant differences in the nucleotide‐binding properties, but the complex of Val‐tRNA synthetase with EF‐1H was 10 times more active in the poly(U)‐directed binding of Phe‐tRNA phe to ribosomes than EF‐1H. These result strongly suggest that the complex of Val‐tRNA synthetase with EF‐1H is a novel functionally active individual form of EF‐1.

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“…The fraction A synthetase complex was eluted with a linear gradient of KC1 (0-0.4 M). The purified fraction A synthetase complex emerged before valyl-tRNA synthetase was eluted (Godar & Yang, 1988).…”

Section: Methodsmentioning

confidence: 99%

Structural organization of the multienzyme complex of mammalian aminoacyl-tRNA synthetases

Godar

Garcia²,

Jacobo³

et al. 1988

Biochemistry

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The multienzyme complexes of mammalian aminoacyl-tRNA synthetases were purified from rat liver, rabbit liver, and rabbit reticulocytes according to the procedure slightly modified from Kellermann et al. [Kellermann, O., Brevet, A., Tonetti, H., & Waller, J.-P. (1979) Eur. J. Biochem. 99, 541-550]. Three forms of the synthetase complex with slightly different protein compositions were identified, suggesting a microheterogeneity of the synthetase complex. The hydrodynamic properties and the protein composition of the purified complexes were determined. The electron micrographs of the complex showed mostly amorphous particles and some hollow rings with an outer diameter of 164 A and an inner diameter of 42 A. The predicted hydrodynamic properties of several models of the complex were calculated. The properties of a ring model appear to best fit with those of the synthetase complex.

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Mammalian high-molecular-weight and monomeric forms of valyl-tRNA synthetase

Cited by 12 publications

References 35 publications

Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation

Elongation factor-1 messenger-RNA levels in cultured cells are high compared to tissue and are not drastically affected further by oncogenic transformation

Purification and properties of a high‐molecular‐mass complex between Val‐tRNA synthetase and the heavy form of elongation factor 1 from mammalian cells

Structural organization of the multienzyme complex of mammalian aminoacyl-tRNA synthetases

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