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A carboxy-terminal pro-sequence of aqualysin I prevents proper folding of the protease domain on its secretion by Saccharomyces cerevisiae

Authors
 Kim DW  ;  Lin SJ  ;  Morita S  ;  Terada I  ;  Matsuzawa H 
Citation
 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, Vol.231(3) : 535-539, 1997 
Journal Title
 BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS 
ISSN
 0006-291X 
Issue Date
1997
MeSH
Amino Acid Sequence ; Cell Compartmentation ; Endoplasmic Reticulum/metabolism ; Protein Folding* ; Protein Precursors/chemistry ; Protein Precursors/metabolism ; Saccharomyces cerevisiae ; Sequence Deletion ; Serine Endopeptidases/metabolism* ; Structure-Activity Relationship ; Thermus/enzymology
Abstract
The precursor of aqualysin I, a subtilisin-type protease secreted by Thermus aquaticus, consists of four domains, an N-terminal signal sequence, an N-terminal pro-sequence, a protease domain, and a C-terminal pro-sequence. A non-covalent N-terminal pro-sequence facilitates the production of active aqualsin I, when the C-terminal pro-sequence is deleted. The role of the C-terminal pro-sequence in protein secretion was analyzed using a Saccharomyces cerevisiae expression system. Deletion of the C-terminal pro-sequence resulted in increased secretion of aqualysin I, i.e., about three times as much as that in the case of the wild type. In the case of the wild-type precursor, non-secreted aqualysin I with the C-terminal pro-sequence was retained in the endoplasmic reticulum in an inactive form, suggesting that the C-terminal pro-sequence prevents the protease domain from taking on a properly folded structure, unlike the N-terminal pro-sequence.
Full Text
https://www.sciencedirect.com/science/article/pii/S0006291X96958994?via%3Dihub
DOI
10.1006/bbrc.1996.5899
Appears in Collections:
1. College of Medicine (의과대학) > Dept. of Physiology (생리학교실) > 1. Journal Papers
Yonsei Authors
Kim, Dong Wook(김동욱) ORCID logo https://orcid.org/0000-0002-5025-1532
URI
https://ir.ymlib.yonsei.ac.kr/handle/22282913/177267
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