Structure and partial amino acid sequence of calf thymus DNA topoisomerase II: comparison with other type II enzymes
Autor: | Caroline A. Austin, E. E. C. Margerrison, Paul T. Wingfield, L. M. Fisher, Gerardo Turcatti, H. A. Barot, M. V. Hayes |
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Rok vydání: | 1990 |
Předmět: |
Molecular Sequence Data
Biophysics Thymus Gland Biology Biochemistry Isozyme Type II Epitope Homology (biology) chemistry.chemical_compound Epitopes Saccharomyces Complementary DNA Animals Humans Amino Acid Sequence Molecular Biology Peptide sequence chemistry.chemical_classification Topoisomerase Cell Biology Molecular biology Molecular Weight dna topoisomerase (atp hydrolysing) Enzyme DNA Topoisomerases Type II chemistry biology.protein Cyanogen bromide Cattle Drosophila DNA Topoisomerases |
Zdroj: | Biochemical and biophysical research communications. 170(2) |
ISSN: | 0006-291X |
Popis: | The partial amino acid sequence of p140 calf thymus DNA topoisomerase II was determined by analysis of cyanogen bromide peptides. Five peptides were aligned and shared extensive homology with sequences derived from cDNA clones for the human topoisomerase II isoenzyme forms. Less homology was seen with the Drosophila, yeast and bacterial type II enzymes. Calf and human enzymes shared epitopes allowing isolation of a cDNA clone to human topoisomerase II isoenzyme alpha. Our results indicate that calf thymus p140 topoisomerase II is an active N-terminal proteolytic fragment of the native p180 enzyme and demonstrate that mammalian type II enzymes exhibit close sequence similarity. |
Databáze: | OpenAIRE |
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