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Science 27 October 1989:
Vol. 246. no. 4929, pp. 482 - 486
DOI: 10.1126/science.2683070
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Articles

Science, Vol 246, Issue 4929, 482-486
Copyright © 1989 by American Association for the Advancement of Science

articles

Intracellular targeting and structural conservation of a prohormone-processing endoprotease

RS Fuller, AJ Brake, and J Thorner

Department of Biochemistry, University of California, Berkeley 94720.

The prohormone-processing endoprotease (KEX2 gene product) of the yeast Saccharomyces cerevisiae is a membrane-bound, 135,000-dalton glycoprotein, which contains both asparagine-linked and serine- and threonine-linked oligosaccharide and resides in a secretory compartment. Analysis of mutant kex2 genes truncated at their 3' end indicates that carboxyl terminal domains of the enzyme are required for its proper localization within the cell. A human gene product, "furin," shares 50% identity with the catalytic domain of Kex2 protease and is, therefore, a candidate for a human prohormone-processing enzyme.


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