Protein Kinase of Bacteriophage T7

Pai, S. H.; Rahmsdorf, Hans J.; Ponta, Helmut; Hirsch‐Kauffmann, Monica; Herrlich, Peter; Schweiger, Manfred

doi:10.1111/j.1432-1033.1975.tb02164.x

Cited by 35 publications

(12 citation statements)

References 13 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Since T7PK obtained in this manner is phosphorylated ([8] and vide infra ) it is referred to as H-pT7PK, with ‘H’ and ‘p’ referring to the His-tag and phosphate group(s), respectively. Since a previous study indicated that phosphorylation reduces T7PK catalytic activity [7], a method was developed to dephosphorylate H-pT7PK, as well as remove the His-tag, which also could affect activity. H-pT7PK was treated with lambda phage protein phosphatase [20], which has a broad specificity for protein phosphomonoester groups [21,22], then subjected to Ni 2+ -NTA affinity chromatography, providing H-T7PK in a yield of ~10%.…”

Section: Resultsmentioning

confidence: 99%

“…The N-terminal domain possesses T7PK activity, while the SO activity is associated with the C-terminal region, and represses transcription by an unknown mechanism that is independent of T7PK activity [6]. T7PK uses ATP as phosphate donor and requires Mg 2+ as a cofactor [7]. The T7PK domain of the 0.7 gene has been separately cloned and the polypeptide expressed in recombinant form [8].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

Bacteriophage T7 protein kinase: Site of inhibitory autophosphorylation, and use of dephosphorylated enzyme for efficient modification of protein in vitro

Gone

Nicholson

2012

Protein Expression and Purification

View full text Add to dashboard Cite

Bacteriophage T7 encodes a serine/threonine-specific protein kinase that phosphorylates multiple cellular proteins during infection of Escherichia coli. Recombinant T7 protein kinase (T7PK), normally purified in phosphorylated form, exhibits a modest level of phosphotransferase activity. A procedure is described that provides dephosphorylated T7PK with an enhanced ability to phosphorylate protein substrates, including translation initiation factor IF1 and the nuclease domain of ribonuclease III. Mass spectrometric analysis identified Thr12 as the site of IF1 phosphorylation in vitro. T7PK undergoes Mg2+-dependent autophosphorylation on Ser216 in vitro, which also is modified in vivo. The inability to isolate the presumptive autophosphorylation-resistant T7PK Ser216Ala mutant indicates a toxicity of the phosphotransferase activity and suggests a role for Ser216 modification in limiting T7PK activity during infection.

show abstract

Section: Resultsmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Bacteriophage T7 protein kinase: Site of inhibitory autophosphorylation, and use of dephosphorylated enzyme for efficient modification of protein in vitro

Gone

Nicholson

2012

Protein Expression and Purification

View full text Add to dashboard Cite

show abstract

“…The reasons for and functions of local polymorphisms of the proteins are unclear, but they can be explained in part by evolution for optimal interaction with host proteins. gp0.7 is a serine/threonine protein kinase and phosphorylates translational components (IF1, IF2, IF3, elongation factor G, and ribosomal proteins S1 and S6), host RNAP ␤Ј subunit, and enzymes related to mRNA metabolism (RNase III and RNase E), resulting in exclusive phage gene expression (41,43,48,55,57,58,65,81). gp6 is an exonuclease and contributes to the packaging of concatemerized phage DNA by suppressing the packaging of host DNA (69).…”

Section: Vol 74 2008 Characterization Of a T7-like Virus (Sg-jl2) 6975mentioning

confidence: 99%

Characterization of a T7-Like Lytic Bacteriophage (φSG-JL2) of Salmonella enterica Serovar Gallinarum Biovar Gallinarum

Kwon

Cho²,

Kim

et al. 2008

Appl Environ Microbiol

View full text Add to dashboard Cite

SG-JL2 is a newly discovered lytic bacteriophage infecting Salmonella enterica serovar Gallinarum biovar Gallinarum but is nonlytic to a rough vaccine strain of serovar Gallinarum biovar Gallinarum (SG-9R), S. enterica serovar Enteritidis, S. enterica serovar Typhimurium, and S. enterica serovar Gallinarum biovar Pullorum. The SG-JL2 genome is 38,815 bp in length (GC content, 50.9%; 230-bp-long direct terminal repeats), and 55 putative genes may be transcribed from the same strand. Functions were assigned to 30 genes based on high amino acid similarity to known proteins. Most of the expected proteins except tail fiber (31.9%) and the overall organization of the genomes were similar to those of yersiniophage YeO3-12. SG-JL2 could be classified as a new T7-like virus and represents the first serovar Gallinarum biovar Gallinarum phage genome to be sequenced. On the basis of intraspecific ratios of nonsynonymous to synonymous nucleotide changes (Pi[a]/Pi[s]), gene 2 encoding the host RNA polymerase inhibitor displayed Darwinian positive selection. Pretreatment of chickens with SG-JL2 before intratracheal challenge with wild-type serovar Gallinarum biovar Gallinarum protected most birds from fowl typhoid. Therefore, SG-JL2 may be useful for the differentiation of serovar Gallinarum biovar Gallinarum from other Salmonella serotypes, prophylactic application in fowl typhoid control, and understanding of the vertical evolution of T7-like viruses.

show abstract

“…The enzyme has maximal activity at 6 min after infection at 37°C, after which it rapidly declines to near preinfection levels. Various T5 phage-induced functions inhibit or modify host activities (7,17,18), and a T7 phageinduced enzyme, in effect, self-destructs (13).…”

mentioning

confidence: 99%

Properties of deoxynucleoside 5'-monophosphatase induced by bacteriophage T5 after infection of Escherichia coli

Mozer¹,

Warner²

1977

J Virol

View full text Add to dashboard Cite

Bacteriophage T5 induced a deoxynucleoside 5'-monophosphatase during its infection of Escherichia coli. The enzyme was purified about 100-fold. It was clearly distinct from the host 5'-nucleotidase activity in its physical characteristics and substrate specificity. The enzyme was active on deoxynucleoside 5'-monophosphates but was not active as a phosphatase on ribonucleotides, deoxynucleoside 5'-triphosphates, deoxynucleoside 3'-monophosphates, or deoxyoligonucleotides. Furthermore, it did not have oligonucleotidase or exonuclease activity. The enzyme could exist in multimeric form but had a monomer molecular weight of about 25,000.

show abstract

Protein Kinase of Bacteriophage T7

Cited by 35 publications

References 13 publications

Bacteriophage T7 protein kinase: Site of inhibitory autophosphorylation, and use of dephosphorylated enzyme for efficient modification of protein in vitro

Bacteriophage T7 protein kinase: Site of inhibitory autophosphorylation, and use of dephosphorylated enzyme for efficient modification of protein in vitro

Characterization of a T7-Like Lytic Bacteriophage (φSG-JL2) of Salmonella enterica Serovar Gallinarum Biovar Gallinarum

Properties of deoxynucleoside 5'-monophosphatase induced by bacteriophage T5 after infection of Escherichia coli

Contact Info

Product

Resources

About