Chemical studies on methionyl-tRNA synthetase from Escherichia coli

Bruton, Chris J.; Hartley, Brian

doi:10.1016/0022-2836(70)90023-9

Cited by 308 publications

(64 citation statements)

References 30 publications

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“…A similar effect is observed upon binding of Mg 2+ to tR2JA I~te [ 12]. This phenomenon has been interpreted as a shielding of the Y-base against the quenching effect of water molecules.…”

Section: Oiset~sioasupporting

confidence: 55%

Thermodynamics and kinetics of the interaction of phenylalanine‐specific tRNA from yeast with its cognate synthetase as studied by the flourescence of the Y‐base

Krauss¹,

Römer²,

Riesner³

et al. 1973

FEBS Letters

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“…A similar effect is observed upon binding of Mg 2+ to tR2JA I~te [ 12]. This phenomenon has been interpreted as a shielding of the Y-base against the quenching effect of water molecules.…”

Section: Oiset~sioasupporting

confidence: 55%

Thermodynamics and kinetics of the interaction of phenylalanine‐specific tRNA from yeast with its cognate synthetase as studied by the flourescence of the Y‐base

Krauss¹,

Römer²,

Riesner³

et al. 1973

FEBS Letters

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“…From each second fraction, aliquots were removed and dried. In the initial stages of the work the amino-terminal residues of the peptides present in the fractions were determined manually by the Dansyl technique (Bruton and Hartley, 1970). Fractions that contained peptide material of interest were dried and subjected to reverse-phase HPLC separation on a Nucleosil C18 column (0.4 cm x 25 cm), operated in 0.08% trifluoroacetic acid.…”

Section: Separation Of Proteolytic Peptidesmentioning

confidence: 99%

Chemical cross‐linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher‐level complex between protofilaments

Geisler

Schünemann

Weber

1992

European Journal of Biochemistry

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Tetrameric rods, protofilaments and assembled filaments of desmin, the intermediate filament protein of muscle, have been chemically cross-linked with the lysine specific cross-linkers EGS [ethylene glycol bis(succinimidylsuccinate), 1.61 nm span] and bis(sulfosuccinimidy1) suberate (1 .I4 nm span). One bis(sulfosuccinimidy1)suberate and two EGS cross-links were isolated from the rod and characterized. They show that the two coiled coils in the rod tetramer are staggered by approximately 15-20 nm and strongly indicate an antiparallel arrangement in which the inner overlapping part of the rod is formed by the amino-terminal helices lA, 1B and 2A. Both EGS crosslinks identified in the rod were also isolated from cross-linked filaments. The isolated rod, therefore, represents a complex also present in identical, or very similar form in protofilaments and in assembled filaments. Cross-linked filaments yielded a third EGS cross-link that must have been formed between neighboring protofilaments. It connects the highly conserved carboxy-terminus of helix 2B of the f i s t protofilament to the overlap region formed by helices 1A and 2A of the second protofilament. The restrictions posed by these cross-links on current filament models are discussed.

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“…8). According to Bruton and Hartley [19], the stoichiometry of the complex formed can be obtained from the intersection of the extrapolation of the initial slope of the quenching curve with the base line reached a t high tRNAArg concentrations. Fig.…”

Section: Fluorescence Measurementsmentioning

confidence: 99%

Specific Modification of Arginyl‐Transfer Ribonucleic‐Acid Synthetase from Bacillus stearothermophilus as a Result of Substrate Binding

Parfait¹

1973

European Journal of Biochemistry

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The association between arginyl-tRNA synthetase from Bacillus stearothermophilus and tRNAArg was studied. ARP does not change the equilibrium of this association. The K , values for homologous tRNA and tRNA from Escherichia coli, and the inhibition constant ( K i ) for periodate-oxidized tRNA were determined.The synergistic protection of arginyl-tRNA synthetase against heat inactivation, induced by tRNAArg, ATP and arginine, occurs in two discrete steps, the first being observed when the enzyme is incubated in the presence of tRNAArg and ATP, the second in the additional presence of arginine. With periodate-oxidized tRNA, only the first step is observed.Arginyl-tRNA synthetase dimerizes in the presence of tRNA species which can be aminoacylated by the enzyme. An effect of ATP on the kinetic parameters of enzyme-tRNA association was indicated.Fluorescence measurements show that one molecule of tRNAArg is bound per molecule of enzyme monomer (Nr 78000).It is concluded from these and previous results, that an intermediary complex composed of the enzyme h e r , to which two molecules of each substrate (tRNAArg, ATP, arginine) have been bound in an ordered sequence, forms prior to the aminoacylation reaction catalysed by the enzyme.

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Chemical studies on methionyl-tRNA synthetase from Escherichia coli

Cited by 308 publications

References 30 publications

Thermodynamics and kinetics of the interaction of phenylalanine‐specific tRNA from yeast with its cognate synthetase as studied by the flourescence of the Y‐base

Thermodynamics and kinetics of the interaction of phenylalanine‐specific tRNA from yeast with its cognate synthetase as studied by the flourescence of the Y‐base

Chemical cross‐linking indicates a staggered and antiparallel protofilament of desmin intermediate filaments and characterizes one higher‐level complex between protofilaments

Specific Modification of Arginyl‐Transfer Ribonucleic‐Acid Synthetase from Bacillus stearothermophilus as a Result of Substrate Binding

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