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PubMed1969

Polynucleotide ligase activity in cells infected with simian virus 40, polyoma virus, or vaccinia virus.

The conversion of simian virus 40 (SV40) component II deoxyribonucleic acid to component I has been used to assay polynucleotide ligase in extracts of tissue culture cells. All cell types examined, including chicken, hamster, mouse, monkey, and human cells, contained adenosine triphosphate-dependent ligase. After infection of mouse embryo, monkey kidney, and HeLa cells with polyoma virus, SV40, and vaccinia virus, respectively, the enzyme activity increased, but its cofactor requirement was unchanged. In vaccinia virus-infected cells, the increased activity was localized in the cytoplasm. Ligase induction occurred in the presence of cytosine arabinoside but was prevented by puromycin. Rifampicin blocked the production of infectious vaccinia particles but had little effect on the induction of ligase.

Animals↗
PubMed1994

Covalent catalysis in nucleotidyl transfer reactions: essential motifs in Saccharomyces cerevisiae RNA capping enzyme are conserved in Schizosaccharomyces pombe and viral capping enzymes and among polynucleotide ligases.

Formation of the 5' cap structure of eukaryotic mRNAs occurs via transfer of GMP from GTP to the 5' terminus of the primary transcript. RNA guanylyltransferase, the enzyme that catalyzes this reaction, has been isolated from many viral and cellular sources. Though differing in molecular weight and subunit structure, the various guanylyltransferases employ a common catalytic mechanism involving a covalent enzyme-(Lys-GMP) intermediate. Saccharomyces cerevisiae CEG1 is the sole example of a cellular capping enzyme gene. In this report, we describe the identification and characterization of the PCE1 gene encoding the capping enzyme from Schizosaccharomyces pombe. PCE1 was isolated from a cDNA library by functional complementation in Sa. cerevisiae. Induced expression of PCE1 in bacteria and in yeast confirmed that the 47-kDa Sc. pombe protein was enzymatically active. The amino acid sequence of PCE1 is 38% identical (152 of 402 residues) to the 52-kDa capping enzyme from Sa. cerevisiae. Comparison of the two cellular capping enzymes with guanylyltransferases encoded by DNA viruses revealed local sequence similarity at the enzyme's active site and at four additional collinear motifs. Mutational analysis of yeast CEG1 demonstrated that four of the five conserved motifs are essential for capping enzyme function in vivo. Remarkably, the same motifs are conserved in the polynucleotide ligase family of enzymes that employ an enzyme-(Lys-AMP) intermediate. These findings illuminate a shared structural basis for covalent catalysis in nucleotidyl transfer and suggest a common evolutionary origin for capping enzymes and ligases.

Amino Acid Sequence↗
PubMed1982

Increased activity of polynucleotide ligase in 5-iodo-2'-deoxyuridine and mitomycin C-pretreated simian virus 40 (SV40)-infected monkey kidney cells.

The DNA ligase activity has been studied in 5-iodo-2'-deoxyuridine (IUdR), mitomycin C (MMC) and IUdR + MMC-treated SV40-infected or mock-infected CV1C11 monkey kidney cells. The results have shown that : 1. The level of enzyme activity is about two or three times higher in IUdR or MMC-treated non-infected cells; 2. SV40 infection doubles the level of ligase activity in the untreated cells; 3. There is an additional increase of ligase activity in IUdR or MMC-treated SV40-infected cells; 4. When infected or mock-infected cells are treated with IUdR + MMC, there is no modification of the results obtained with each drug alone; 5. Two peaks of different S values are detected in a partial purification of the drug(s) or viral induced enzyme(s). The increase in the ligase activity in drug-treated cells is independent of semi-conservative DNA synthesis. The drug(s) and viral-induced enzyme(s) is the consequence of a "de novo" synthesis of proteins, as shown by cycloheximide treatment.

Animals↗