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Murine and human cathepsin Z: cDNA-cloning, characterization of the genes and chromosomal localization
J Deussing1, I von Olshausen, C Peters
1Institut für Molekulare Medizin und Zellforschung, Klinikum der Albert-Ludwigs-Universität Freiburg, Hugstetter Strasse 55, 79106, Freiburg, Germany.
Abstract:
A novel murine cysteine protease from the family of papain-like cysteine proteinases was identified by dbEST-database search. A 1. 4-kb full-length cDNA encoding a predicted polypeptide of 306 amino acids was characterized. The new protease, tentatively named cathepsin Z, exhibits all features characteristics of a papain-like cysteine protease, including the highly conserved residues of the 'catalytic triad'. Cathepsin Z shares only 26-35% overall homology with previously described mammalian papain-like cysteine peptidases and has an unusually short propeptide, which may indicate that it is a member of a putative new subfamily within the family of papain-like cysteine peptidases. Genomic clones covering the murine and human cathepsin Z genes were isolated. They comprise six exons and five introns spanning a 12-kb region of genomic DNA, respectively. Murine cathepsin Z was mapped to chromosome 2, a region with synteny homology to a region of human chromosome 20 to which human cathepsin Z has been mapped previously. Northern blot analysis revealed ubiquitous expression of murine cathepsin Z. Multiple transcriptional start sites were identified for the murine cathepsin Z gene and together with the absence of a TATA box, a high G+C content, a CpG island and the presence of several Sp1-binding sites in the promoter region, murine cathepsin Z may be classified as a 'housekeeping' gene.
Insights
A novel cysteine protease, cathepsin Z, was identified in mice. This papain-like cysteine proteinase exhibits unique characteristics and widespread gene expression, suggesting a housekeeping function.
Area of Science:
- Biochemistry
- Genetics
- Molecular Biology
Background:
- Papain-like cysteine proteases are a significant family of enzymes.
- Understanding novel members of this family is crucial for biological research.
Purpose of the Study:
- To identify and characterize a novel murine cysteine protease.
- To investigate the genetic structure, localization, and expression of this new enzyme, named cathepsin Z.
Main Methods:
- dbEST database search for novel protein sequences.
- cDNA sequencing and amino acid prediction.
- Homology analysis with known proteases.
- Gene structure analysis using genomic clones.
- Chromosomal mapping.
- Northern blot analysis for gene expression profiling.
Main Results:
- A novel murine cysteine protease, cathepsin Z, was identified with characteristic papain-like features.
- Cathepsin Z shows low homology to other mammalian peptidases and possesses a short propeptide, suggesting a new subfamily.
- The cathepsin Z gene comprises six exons and five introns.
- Murine cathepsin Z is located on chromosome 2, with synteny to human chromosome 20.
- Ubiquitous expression of murine cathepsin Z was observed, with multiple transcriptional start sites and a TATA-box-deficient promoter.
Conclusions:
- Cathepsin Z represents a novel member of the papain-like cysteine protease family.
- Its unique structural features and ubiquitous expression indicate a potential housekeeping role.
- Further research into cathepsin Z functions is warranted.
