Tissue-specific splicing of Omi stress-regulated endoprotease leads to an inactive protease with a modified PDZ motif

    Authors

    L. Faccio; C. Fusco; A. Viel;A. S. Zervos

    Comments

    Authors: contact us about adding a copy of your work at STARS@ucf.edu

    Abbreviated Journal Title

    Genomics

    Keywords

    CHROMOSOME 2P13; DNA-BINDING; TRANSLOCATION; GENE; RECOGNITION; GENERATION; ACTIVATION; LEUKEMIA; HOMOLOG; CLONING; Biotechnology & Applied Microbiology; Genetics & Heredity

    Abstract

    Omi is a human serine protease whose catalytic domain is homologous to a bacterial heat shock endoprotease (HtrA), a protein indispensable to the survival of bacteria at elevated temperatures. Omi is expressed ubiquitously, and its protein product is predominantly localized in the endoplasmic reticulum of mammalian cells. Here we present the genomic structure of Omi, consisting of eight exons located on human chromosome 2p12-p13. Furthermore, we describe an alternatively splice form of Omi (D-Omi) that is expressed predominantly in the kidney, colon, and thyroid. D-Omi lacks peptide sequence encoded by two exons (exons III and VII). The absence of exon VII leads to a protein with a modified PDZ domain unable to interact with a known partner, the Mxi2 protein. The absence of exon III affects the catalytic domain and leads to a protein with no detectable protease activity. Our studies suggest that D-Omi may have a unique role in the normal function of kidney, colon, and thyroid. (C) 2000 Academic Press.

    Journal Title

    Genomics

    Volume

    68

    Issue/Number

    3

    Publication Date

    1-1-2000

    Document Type

    Article

    Language

    English

    First Page

    343

    Last Page

    347

    WOS Identifier

    WOS:000089549900014

    ISSN

    0888-7543

    Share

    COinS