Mammalian cells contain a second nucleocytoplasmic hexosaminidase

Author:

Gutternigg Martin1,Rendić Dubravko1,Voglauer Regina2,Iskratsch Thomas3,Wilson Iain B. H.1

Affiliation:

1. Department für Chemie, Universität für Bodenkultur, Muthgasse 18, A-1190 Wien, Austria

2. Institut für angewandte Mikrobiologie, Universität für Bodenkultur, Muthgasse 18, A-1190 Wien, Austria

3. Randall Division for Cell and Molecular Biophysics and Cardiovascular Division, King's College, London SE1 1UL, U.K.

Abstract

Some thirty years ago, work on mammalian tissues suggested the presence of two cytosolic hexosaminidases in mammalian cells; one of these has been more recently characterized in a recombinant form and has an important role in cellular function due to its ability to cleave β-N-acetylglucosamine residues from a variety of nuclear and cytoplasmic proteins. However, the molecular nature of the second cytosolic hexosaminidase, named hexosaminidase D, has remained obscure. In the present study, we molecularly characterize for the first time the human and murine recombinant forms of enzymes, encoded by HEXDC genes, which appear to correspond to hexosaminidase D in terms of substrate specificity, pH dependency and temperature stability. Furthermore, a Myc-tagged form of this novel hexosaminidase displays a nucleocytoplasmic localization. Transcripts of the corresponding gene are expressed in a number of murine tissues. On the basis of its sequence, this enzyme represents, along with the lysosomal hexosaminidase subunits encoded by the HEXA and HEXB genes, the third class 20 glycosidase to be identified from mammalian sources.

Publisher

Portland Press Ltd.

Subject

Cell Biology,Molecular Biology,Biochemistry

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