Ribosomes after infection with bacteriophage T4 and T7

Rahmsdorf, Hans J.; Herrlich, Peter; Pai, S. H.; Schweiger, Manfred; Wittmann, H. G.

doi:10.1007/bf00333766

Cited by 46 publications

(17 citation statements)

References 16 publications

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“…It is unclear whether the T7 protein kinase is multifunctional, however, because the phosphorylation in vivo of some of its substrates (e.g. ribosomes) appears to be gratuitous, in a similar manner to that found with the sre protein kinase (Rahmsdorf et al, 1973). The function of this enzyme still needs to be clarified, and studies using the cloned 0.7 gene will no doubt provide some of the answers.…”

Section: Bacteriophage T7 Protein Kinasementioning

confidence: 99%

Viral Aspects of Protein Phosphorylation

Leader

Katan

1988

Journal of General Virology

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Section: Bacteriophage T7 Protein Kinasementioning

confidence: 99%

Viral Aspects of Protein Phosphorylation

Leader

Katan

1988

Journal of General Virology

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“…In our previous work on phage T7, we reported that labeled phosphate is incorporated into ribosomal protein after T7 infection (6,23 were then subject to SDS slab-gel electrophoresis (9); the gels were dried and placed on x-ray film overnight. Assay for Protein Kinase In Vitro.…”

Section: Introductionmentioning

confidence: 99%

“…This rapidity of change in gene expression prompted our search for group transfers after phage infection (4-6). A phage-induced group transfer to components of the existing host machinery of gene expression would allow both a fast and an economical control.In our previous work on phage T7, we reported that labeled phosphate is incorporated into ribosomal protein after T7 infection (6,23 were then subject to SDS slab-gel electrophoresis (9); the gels were dried and placed on x-ray film overnight. Assay for Protein Kinase In Vitro.…”

mentioning

confidence: 99%

“…One particular aspect of these systems is the rapidity of changes in the pattern of gene expression; phage T7 induces a whole series of control mechanisms within [4][5] min (2,3). This rapidity of change in gene expression prompted our search for group transfers after phage infection (4)(5)(6). A phage-induced group transfer to components of the existing host machinery of gene expression would allow both a fast and an economical control.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Protein Kinase Induction in Escherichia coli by Bacteriophage T7

Rahmsdorf¹,

Pai²,

Ponta³

et al. 1974

Proc. Natl. Acad. Sci. U.S.A.

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117

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After bacteriophage T7 infection, a protein kinase (EC 2.7.1.37; ATP:protein phosphotransferase) activity can be demonstrated in E. coli in vivo by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and autoradiography. Cell-free extracts catalyzed the transfer of the terminal phosphoryl group of [-y_32P]ATP to endogenous protein acceptor or to added histone. The bond between phosphate and protein shows the characteristies of serine phosphate: it is stable in 1 N HCl (1000) and cleaved by 1 N KOH (370) and by alkaline phosphatase treatment. Moreover, after partial acid hydrolysis, radiophosphate migrates with marker O-phosphoserine on polyethyleneimine-cellulose thin-layer chromatograms. Enzyme activity in uninfected cells is negligible. Ultraviolet irradiation of the phage genome prevents the appearance of the protein kinase; irradiation of the host genome does not. The enzyme activity occurs 4 min after infection and its gene maps in the early region (promoter proximal to gene 1). Ribosomal proteins are phosphorylated in vivo and are substrates in vitro. Enzyme activity in vitro is not changed by addition of cyclic AMP or cyclic GMP.Bacteriophage systems have been used extensively to study the regulation of gene expression (1,2). One particular aspect of these systems is the rapidity of changes in the pattern of gene expression; phage T7 induces a whole series of control mechanisms within 4-5 min (2, 3). This rapidity of change in gene expression prompted our search for group transfers after phage infection (4-6). A phage-induced group transfer to components of the existing host machinery of gene expression would allow both a fast and an economical control.In our previous work on phage T7, we reported that labeled phosphate is incorporated into ribosomal protein after T7 infection (6,23 were then subject to SDS slab-gel electrophoresis (9); the gels were dried and placed on x-ray film overnight. Assay for Protein Kinase In Vitro. Brij-lysozyme cell extracts (10) were used as enzyme sources. The incubations were carried out at 300 for 5 min in a total volume of 0.1 ml. The incubation mixtures contained 30A]. of cell extract, 3 mg/ml of type II histone, and either (1) 15 mM sodium phosphate (pH 7.0), 0.01 MMgCl2, 0.14 mM ATP (35.7 Ci ['y32-P]ATP/mol) or (2) 25 mM Tris HCl (pH 7.0), 5 mM MgCI2, 0.1 mM EDTA, 44,AM, ATP (114 Ci of [32P]ATP/mol). The incubations were started by the addition of enzyme (cell extract) and stopped by addition of 1.5 ml of 10% trichloroacetic acid.The precipitates were boiled in trichloroacetic acid for 15 min, chilled in ice for 10 min, and collected on glass-fiber filter discs. The discs were washed 5 times with 10 ml of 10% trichloroacetic acid and once with 10 ml of methanol. After the filters were dried, radioactivity on the filters was measured by liquid scintillation spectrometry. In selected experiments, the 10% trichloroacetic acid suspensions of precipitate were heated to 900 for 20 min, cooled to ambient temperature, and centrifuged at 2500 X g. These precipit...

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“…In procaryotic cells, a similar regulation system has been found in Escherichia coli cells infected with bacteriophage T7 (16,22,23,25). Recently, much evidence for the existence of protein kinases has been obtained with E. coli cells (4,17).…”

mentioning

confidence: 64%

Participation of the dnaK and dnaJ gene products in phosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase of Escherichia coli K-12

Wada¹,

Sekine²,

Itikawa³

1986

J Bacteriol

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The heat shock proteins DnaK and DnaJ of Escherichia coli participate in phosphorylation of both glutaminyl-tRNA synthetase and threonyl-tRNA synthetase. When cellular proteins extracted from the dnaK7(Ts) and dnaJ259(Ts) mutant cells labeled with 32Pi at 42°C were analyzed by two-dimensional gel electrophoresis, no phosphorylation of these proteins was observed when they were compared with those from wild-type cells.

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Ribosomes after infection with bacteriophage T4 and T7

Cited by 46 publications

References 16 publications

Viral Aspects of Protein Phosphorylation

Viral Aspects of Protein Phosphorylation

Protein Kinase Induction in Escherichia coli by Bacteriophage T7

Participation of the dnaK and dnaJ gene products in phosphorylation of glutaminyl-tRNA synthetase and threonyl-tRNA synthetase of Escherichia coli K-12

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