• Publications
  • Influence
Pyrophosphatase is essential for growth of Escherichia coli
The ppa gene for inorganic pyrophosphatase is essential for the growth of Escherichia coli. A recombinant with a chromosomal ppa::Kanr lesion and a temperature-sensitive replicon with a ppa+ geneExpand
Structural studies of lysyl-tRNA synthetase: conformational changes induced by substrate binding.
The crystal structure of the constitutive lysyl-tRNA synthetase (LysS) from Escherichia coli has been determined to 2.7 A resolution in the unliganded form and in a complex with the lysine substrate. Expand
Catabolism of bis(5'-nucleosidyl) oligophosphates in Escherichia coli: metal requirements and substrate specificity of homogeneous diadenosine-5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase.
Diadenosine-5',5'''-P1,P4-tetraphosphate pyrophosphohydrolase (diadenosinetetraphosphatase) from Escherichia coli strain EM20031 has been purified 5000-fold from 4 kg of wet cells. It produces 2.4 mgExpand
Yeast diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase behaves as a dinucleoside tetraphosphate synthetase.
The diadenosine 5',5'''-P1,P4-tetraphosphate alpha,beta-phosphorylase, recently observed in yeast, is shown to be capable of catalyzing the synthesis of Ap4A from ATP + ADP, i.e., the reverse reaction of the phosphorolysis ofAp4A. Expand
Control of 5′,5′-Dinucleoside Triphosphate Catabolism by APH1, a Saccharomyces cerevisiaeAnalog of Human FHIT
It is shown that the Saccharomyces cerevisiae APH1 gene product, which resembles human Fhit protein, also hydrolyzes dinucleoside 5',5'-polyphosphates, with Ap3A being the preferred substrate. Expand
Zinc-dependent synthesis of 5',5'-diadenosine tetraphosphate by sheep liver lysyl- and phenylalanyl-tRNA synthetases.
Observation made with aminoacyl-tRNA synthetases of mammalian origin supports the proposal that changes in cellular free zinc ion concentration could contribute to 5',5'-diadenosine tetraphosphate variations in animal cells as a function of growth activity. Expand
Myosin synthesis increased by electrical stimulation of skeletal muscle cell cultures.
In a culture system of skeletal muscle cells that have differentiated in the absence of innervation, one can elicit the protein synthetic response associated with skeletal muscle hypertrophy in vivo. Expand
Yeast 3‐Phosphoglycerate Kinase
The mechanism of the transphosphorylation reaction catalyzed by yeast 3-phosphoglycerate kinase has been studied by means of spectrophotometric investigations. The binding sites, one for theExpand
Non-adenylylated bis(5'-nucleosidyl) tetraphosphates occur in Saccharomyces cerevisiae and in Escherichia coli and accumulate upon temperature shift or exposure to cadmium.
A new set of bis(5'-nucleosidyl) tetraphosphates, the Bp4B' nucleotides (B and B' = C, G, or U not equal to A), are demonstrated in living cells and are likely to originate from the action of diadenosine-5',5"'-P1,P4-tetraphosphate alpha,beta-phosphorylase, an enzyme recently found in yeast. Expand
Yeast hexokinase: interaction with substrates and analogs studied by difference spectrophotometry.
Spectrophotometric studies evidence the formation of a binary complex and ternary complexes (sugar · enzyme · nucleotide) in accord with an ordered mechanism. Expand