The chloromethylketone protease inhibitor AAPFCMK also targets ATP-dependent helicases and SAP-domain proteins

Chetan Dhamne, David A. Drubin, Kimberly Duncan, M. Judith Tevethia, Gary Clawson

Research output: Contribution to journalArticlepeer-review

4 Scopus citations

Abstract

We have been studying a nuclear protease, which appears to be involved in cellular transformation, as well as in infections with high-risk human papillomaviruses (HPVs). This protease has a chymotrypsin-like substrate specificity and the chloromethylketone inhibitor AAPFCMK is a potent (and relatively selective) inhibitor of it. Recently, we have observed that AAPFCMK has potent effects in some model systems which appear not to be mediated by decreases in the nuclear protease. Here we show that AAPF CMK selectively reacts with ATP-dependent helicases as well as a limited spectrum of proteins in other DNA repair/chromatin remodeling nuclear complexes, including for example Cohesin complex components and proteins containing SAP-domains. In vitro, AAPFCMK selectively reacts with SV40 large T antigen, and inhibits its helicase activity.

Original languageEnglish (US)
Pages (from-to)716-726
Number of pages11
JournalJournal of cellular biochemistry
Volume100
Issue number3
DOIs
StatePublished - Feb 15 2007

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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