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Organization of the gene encoding the human endothelin-converting enzyme (ECE-1)
O Valdenaire1, E Rohrbacher, M G Mattei
1F. Hoffmann-La Roche Ltd., Pharma Division, Basel, Switzerland.
The Journal of Biological Chemistry
|December 15, 1995
Summary
The human endothelin-converting enzyme (ECE-1) gene produces two isoforms with distinct tissue distributions via separate transcription start sites. This gene structure and phylogenetic analysis reveal a novel metalloprotease subfamily.
Area of Science:
- Molecular Biology
- Genetics
- Biochemistry
Background:
- The human endothelin-converting enzyme (ECE-1) exists in two isoforms, differing in their N-terminal regions.
- These isoforms are encoded by a single gene located on human chromosome 1p36.
Purpose of the Study:
- To characterize the gene structure and regulatory elements of the human ECE-1 gene.
- To investigate the evolutionary relationship of ECE-1 with other metalloproteases.
Main Methods:
- Gene structure analysis (exons, introns, size).
- Mapping the ECE-1 gene to human chromosome 1p36.
- Analysis of mRNA tissue distribution.
- Identification of transcription start sites and promoter regions.
- Phylogenetic analysis of metalloproteases.
Main Results:
- The ECE-1 gene comprises 19 exons spanning over 68 kilobases.
- Two distinct transcription start sites lead to isoform-specific precursor mRNAs with varied tissue distribution.
- Promoter analysis identified motifs for several transcription factors.
- Phylogenetic studies confirm ECE-1 belongs to a distinct metalloprotease subfamily.
Conclusions:
- The human ECE-1 gene exhibits complex regulation through alternative transcription start sites, leading to functionally distinct isoforms.
- The structural and phylogenetic data support the classification of ECE-1 within a specific subfamily of zinc metalloproteases.