Role of lysyl-tRNA in the regulation of lysine biosynthesis in Escherichia coli K12

Boy, Emmanuelle; Reinisch, F; Richaud, Catherine; Patte, Jean‐Claude

doi:10.1016/s0300-9084(76)80372-0

Cited by 12 publications

(4 citation statements)

References 23 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In addition, with AspRS and AsnRS, LysRS forms a subgroup within the class II family . Previous work showed that a lysine bradytroph E. coli strain (OEL134) produced low amounts of LysRS activity and that this low activity was likely to be caused by a mutation in the lysS gene (Boy et al, 1976;Hassani et al, 1991). The origin of this defect is confirmed in the present study.…”

supporting

confidence: 84%

“…Previous work suggested that the lysine bradytroph strain OEL134 of E. coli was mutated in the lysS gene encoding constitutive LysRS (Boy et al, 1976;Hassani et al" 1991).…”

Section: Resultsmentioning

confidence: 99%

“…Bacterial Strains. All bacterial strains used through this work were E. coli K12 derivatives: JM101TR (supE thi (lac-pro) recA56 srl-300::Fnl0 F'(traD36 lacE proAB lacZAM15)) (Hirel et al, 1988), OEL134 (lys-1102) (Boy et al, 1976), and PAL3103SAK (F" A(lac-pro) gyrA rpoB metB argE(am) ara supF AlysS::kan) (Lévéque et al, 1991).…”

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

Commans¹,

Blanquet²,

Plateau³

1995

Biochemistry

View full text Add to dashboard Cite

The constitutive lysyl-tRNA synthetase (LysRS) of the Escherichia coli strain OEL134 differs from the wild-type enzyme by the single substitution of threonine 208 with methionine. In vitro study of the isotopic [32P]PPi-ATP exchange reaction catalyzed by purified T208M LysRS revealed specific features that are not observed with the wild-type LysRS: (i) The steady state of the reaction was reached after a approximately 1-min lag when the addition of the enzyme was used to initiate the reaction. This lag disappeared upon preincubation of the enzyme with lysine and ATP. (ii) The variation of the steady state rate as a function of the lysine concentration in the assay was sigmoidal (Hill coefficient of 1.65), suggesting cooperativity of lysine binding to this dimeric enzyme. The allosteric behavior of the mutant enzyme was further established by showing that, at low concentrations of lysine, low amounts of cadaverine stimulated T208M LysRS activity. T208A LysRS, in which threonine 208 had been changed into alanine by site-directed mutagenesis, displayed the same properties as T208M LysRS. Remarkably, Thr 208 makes part of the first signature motif of class II aminoacyl-tRNA synthetases, a motif likely to be involved in the dimerization of the enzyme subunits. Therefore, the behavior of the Thr 208 mutants of LysRS supports the idea that the dimerization of class II aminoacyl-tRNA synthetases is important for an efficient structuration of their active site.

show abstract

supporting

confidence: 84%

“…Previous work suggested that the lysine bradytroph strain OEL134 of E. coli was mutated in the lysS gene encoding constitutive LysRS (Boy et al, 1976;Hassani et al" 1991).…”

Section: Resultsmentioning

confidence: 99%

See 1 more Smart Citation

A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

Commans¹,

Blanquet²,

Plateau³

1995

Biochemistry

View full text Add to dashboard Cite

show abstract

“…Threonyl-tRNA synthetase was assayed by determining the transfer of -['4C]threonine to acceptor tRNA essentially according to Calendar and Berg (4), with some modifications (1).…”

Section: F101:thr+ Leu+ Gy2615mentioning

confidence: 99%

Threonyl-transfer ribonucleic acid synthetase and the regulation of the threonine operon in Escherichia coli

Johnson¹,

Cohen²,

Saint‐Girons³

1977

J Bacteriol

View full text Add to dashboard Cite

Two threonine-requiring mutants with derepressed expression of the threonine operon were isolated from an Escherichia coli K-12 strain containing two copies of the thr operon. One of them carries a leaky mutation in ilvA (the structural gene for threonine deaminase), which creates an isoleucine limitation and therefore derepression of the thr operon. In the second mutant, the enzymes of the thr operon were not repressed by threonine plus isoleucine; the threonyltransfer ribonucleic acid (tRNA) synthetase from this mutant shows an apparent Km for threonine 200-fold higher than that of the parental strain. The gene, called thrS, coding for threonyl-tRNA synthetase was located around 30 min on the E. coli map. The regulatory properties of this mutant imply the involvement of charged threonyl-tRNA or threonyl-tRNA synthetase in the regulation of the thr operon.

show abstract

Construction of hybrid plasmids containing the lysA gene of Escherichia coli: Studies of expression in Escherichia coli and Saccharomyces cerevisiae

et al. 1981

View full text Add to dashboard Cite

The lysA gene of Escherichia coli has been cloned from a lambda transducing phage on various plasmids, present in different copy numbers in bacterial cells. Synthesis of the product of this gene, diaminopimelate (DAP)-decarboxylase, and its regulation have been studied. Expression does not follow a simple gene dosage effect, maximal expression already being obtained with a six-copy plasmid. This result suggests that either a positive or an autogenous regulatory mechanism is involved. We also used one of the hybrid plasmids to look for expression of the bacterial lysA gene in Saccharomyces cerevisiae. The results indicate that the product of the E. coli gene is not actively translated in yeast.

show abstract

Role of lysyl-tRNA in the regulation of lysine biosynthesis in Escherichia coli K12

Cited by 12 publications

References 23 publications

A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

A Single Substitution in the Motif 1 of Escherichia coli Lysyl-tRNA Synthetase Induces Cooperativity toward Amino Acid Binding

Threonyl-transfer ribonucleic acid synthetase and the regulation of the threonine operon in Escherichia coli

Construction of hybrid plasmids containing the lysA gene of Escherichia coli: Studies of expression in Escherichia coli and Saccharomyces cerevisiae

Contact Info

Product

Resources

About