Literature DB >> 8060534

Human topoisomerase I is phosphorylated in vitro on its amino terminal domain by protein kinase NII.

E Cardellini1, M Bramucci, G L Gianfranceschi, E Durban.   

Abstract

Topoisomerase I purified from HeLa cells was phosphorylated in vitro with protein kinase NII (pkNII) purified from calf thymus: this phosphorylation was inhibited by heparin. A peptide containing a sequence corresponding to a putative pkNII phosphorylation site in topoisomerase I was synthesized and phosphorylated with pkNII. HPLC and two-dimensional analysis show identity between the synthetic phosphorylated peptide and one topoisomerase I phosphopeptide indicating Ser10 as one of the in vitro pkNII phosphorylation sites in topoisomerase I.

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Year:  1994        PMID: 8060534     DOI: 10.1515/bchm3.1994.375.4.255

Source DB:  PubMed          Journal:  Biol Chem Hoppe Seyler        ISSN: 0177-3593


  3 in total

1.  Phosphorylation of serine residues in the N-terminal domains of eukaryotic type I topoisomerases.

Authors:  K Staron; D S Samuels
Journal:  Mol Biol Rep       Date:  1998-07       Impact factor: 2.316

2.  Mitotic phosphorylation stimulates DNA relaxation activity of human topoisomerase I.

Authors:  Jennifer S Hackbarth; Marina Galvez-Peralta; Nga T Dai; David A Loegering; Kevin L Peterson; Xue W Meng; Larry M Karnitz; Scott H Kaufmann
Journal:  J Biol Chem       Date:  2008-04-11       Impact factor: 5.157

Review 3.  Topoisomerases and cancer chemotherapy: recent advances and unanswered questions.

Authors:  Mary-Ann Bjornsti; Scott H Kaufmann
Journal:  F1000Res       Date:  2019-09-30
  3 in total

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