Effect of protein kinase ck2 on topoisomerase I from plasmodia of the slime mold Physarum polycephalum

Relaxing activity of Physarum topoisomerase I was increased by calf thymus protein kinase ck2, similarly as was the activity of mammalian topoisomerase I, despite a pronounced difference between amino-acid sequences of non-conserved domains of Physarum and mammalian enzymes. This feature of Physarum...

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Veröffentlicht in:Acta biochimica polonica 1998-01, Vol.45 (3), p.769-773
Hauptverfasser: Derlacz, R A, Kowalska-Loth, B, Staroń, K
Format: Artikel
Sprache:eng
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Zusammenfassung:Relaxing activity of Physarum topoisomerase I was increased by calf thymus protein kinase ck2, similarly as was the activity of mammalian topoisomerase I, despite a pronounced difference between amino-acid sequences of non-conserved domains of Physarum and mammalian enzymes. This feature of Physarum topoisomerase I was cancelled in nuclear extracts isolated from dibutyryl-cAMP treated plasmodia in which the activity of protein kinase ck2 was elevated.
ISSN:0001-527X
1734-154X
DOI:10.18388/abp.1998_4270