Binding of zinc to Escherichia coli phenylalanyl-tRNA synthetase. Comparison with other aminoacyl-tRNA synthetases

Mayaux, Jean Francois; Blanquet, Sylvain

doi:10.1021/bi00519a020

Cited by 62 publications

(45 citation statements)

References 35 publications

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“…Zinc content was determined by atomic absorption spectroscopy using a Varian AA775 spectrophotometer equipped with an airacetylene burner [15]. Western blot analysis was performed by using specific antibodies against PDF as described [9].…”

Section: General Techniquesmentioning

confidence: 99%

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

et al. 1996

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Upon trypsinolysis, the 18 C-terminal residues of Eschericlria cofi peptide deformylase were removed but the resulting form exhibited full activity. Moreover, a mutant fms gene encoding the first 145 out of the 168 residues of the enzyme was able to complement a fms(Ts) strain and exhibited full activity. Upon progressive truncation up to residue 139, both activity and stability decreased up to complete inactivation. Mutagenesis of residues of the 13g-145 region highlights the importance of Leu-141 and Phe-142. N-Terminal deletions were also carried out. Beyond two residues off, the enzyme showed a dramatic instability. Finally, NMR and thermostability studies of the full-length enzyme and comparison to the 1-147 form strongly suggest that the dispensable residues are disordered in solution.

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Section: General Techniquesmentioning

confidence: 99%

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

et al. 1996

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“…At the same time, these enzymes are able to utilize at least in vitro [4] Ap4A for the formation of aminoacyl adenylate. Besides Ap4A synthesis, Ap3A formation was reported for the same enzymes from the adenylate.enzyme complexes where ADP was generated in the process of Ap4A hydrolysis [6,7]. No aaRS exhibited Ap3A synthesis independent from Ap4 A formation.…”

Section: Introductionmentioning

confidence: 92%

P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

1994

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Bovine tryptophanyl-tRNA synthetase (TrpRS, E.C. 6.1.1.2) is unable to catalyze in vitro formation of Ap4A in contrast to some other aminoacyltRNA synthetases. However, in the presence of L-tryptophan, ATP-Mg 2÷ and ADP the enzyme catalyzes the Ap3A synthesis via adenylate intermediate. Ap3A (not Ap4A) may serve as a substrate for TrpRS in the reaction of E. (Trp ~ AMP) formation and in the tRNA Tw charging. The Km value for Ap3A was higher than the Km for ATP (approx. 1.00 vs. 0.22 mM) and Vm~x was 3 times lower than for ATP. The Zn2+-deficient enzyme catalyzes Ap3A synthesis in the absence of exogenous ADP due to ATPase activity of Zn2+-deprived TrpRS. The inability of mammalian TrpRS to synthesize Ap4A, might be considered as a molecular tool preventing the removal of Zn 2÷ due to chelation by Ap4A and therefore preserving the enzyme activity.

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“…A similar dimeric methionyl-tRNA synthetase of M , 2 x 85 x lo3 can be purified from Bacillus stearothermophilus and again an active monomer of M , 64 x lo3 can be produced by limited subtilisin digestion [5]. All four enzymes have been demonstrated to contain one zinc atom/polypeptide chain [6,7]. The zinc is tightly bound: it is not lost in purification nor by chromatography on Sephadex G-50 nor on overnight dialysis against 0.1 mM EDTA or 204 Chelex.…”

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confidence: 99%

“…the specific aminoacylation of tRNAs, these enzymes do not all contain zinc. E. coli isoleucyl-tRNA synthetase [7] Abbreviarion. Hcpcs, 4-(2-hydroxyethyl)-l-piperazineethancsulfonic acid.…”

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Removal of the Tightly Bound Zinc from Escherichia coli Trypsin-Modified Methionyl-tRNA Synthetase

Mayaux¹,

Kalogerakos²,

Brito³

et al. 2005

European Journal of Biochemistry

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The study of the behaviour of Escherichia coli methionyl-tRNA synthetase with chelating agents has shown that only 1,lO-phenanthroline has an inhibitory effect on the tRNAM" aminoacylation activity. Under identical buffer conditions the isotopic [32P]PPi-ATP exchange activity is insensitive.Dialysis of the enzyme against 1,lO-phenanthroline causes a slow loss of zinc from the enzyme which is paralleled by an irreversible loss of both the aminoacylation and isotopic exchange activities. The loss of zinc becomes faster upon the addition of small amounts of guanidine hydrochloride to the dialysis buffer containing phenanthroline, presumably by partially unfolding the protein.Studies of the reversible denaturation of the enzyme by 5 M guanidine hydrochloride shows that the inclusion of EDTA produces an enzyme species that has lost both zinc and activity. The inactive apoenzyme prepared in guanidine and EDTA can regain activity by dilution in a zinc-containing buffer.

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Binding of zinc to Escherichia coli phenylalanyl-tRNA synthetase. Comparison with other aminoacyl-tRNA synthetases

Cited by 62 publications

References 35 publications

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

Removal of the Tightly Bound Zinc from Escherichia coli Trypsin-Modified Methionyl-tRNA Synthetase

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Binding of zinc to Escherichia coli phenylalanyl-tRNA synthetase. Comparison with other aminoacyl-tRNA synthetases

Cited by 62 publications

References 35 publications

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

The C‐terminal domain of peptide deformylase is disordered and dispensable for activity

P1, P3‐bis(5′‐adenosyl)triphosphate (Ap3A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase

Removal of the Tightly Bound Zinc from Escherichia coli Trypsin-Modified Methionyl-tRNA Synthetase

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P¹, P³‐bis(5′‐adenosyl)triphosphate (Ap₃A) as a substrate and a product of mammalian tryptophanyl‐tRNA synthetase