@article{b9e42d62560f4936bad34bb7ddaf2909,
title = "Alternative processing of proproteins in aspergilli kexB gene disruptants under hyperosmotic conditions",
abstract = "Disruption of the kexB gene encoding a subtilisin-like processing protease in Aspergillus oryzae and Aspergillus nidulans led to remarkable morphological defects, and these phenotypes were suppressed under hyperosmotic conditions. In this study, we investigated to determine whether non-KexB proteases might complement the in vivo function of KexB in the two Aspergillus kexB disruptants. Neither overexpression of opsA or opsB encoding A. oryzae aspartyl proteases homologous to yeast yapsins (YPS1/2) suppressed the kexB mutation, although yapsins are multicopy suppressors for the yeast kex2 mutation. A. nidulans and A. oryzae kexB disruptants grown under hyperosmotic conditions processed a recombinant fusion protein carrying a synthetic dibasic processing site (Lys-Arg) although the disruptants grown under normal growth conditions did not cleave the site. These results suggest that the two Aspergilli have other potential processing proteases that are induced and/or activated under hyperosmotic conditions and consequently complement, at least in part, the in vivo function of KexB.",
keywords = "Aspergillus nidulans, Aspergillus oryzae, Hyperosmotic stress, KexB (Kex2p-like endoprotease), Processing protease",
author = "Osamu Mizutani and Kentaro Furukawa and Shunsuke Ichiyanagi and Yoshihiko Matsuda and Masafumi Tokuoka and Tomonori Fujioka and Youhei Yamagata and Katsuya Gomi and Keietsu Abe",
note = "Funding Information: We thank Kazuhisa Ono (University of Hiroshima) for providing antibody, and Takahiro Shintani (Tohoku University) for helpful discussion. We also thank Tsuruji Satou, Shinsaku Ohtaki, and Takamitsu Maruyama (Tohoku University) and all the members of Laboratories for Enzymology and Bioindustrial Genomics for their support, advice, and valuable discussion. This work was supported in part by a Grant-in-Aid for Scientific Research in Priority Areas (Applied Genome, no. 17019001) from the Ministry of Education, Culture, Sports, Science, and Technology of Japan. K.A. was supported partly by grants from the Bio-Oriented Technology Research Advancement Institution (BRAIN) and the New Energy and Industry Technology Development Organization (NEDO) of Japan.",
year = "2009",
doi = "10.1271/bbb.80437",
language = "English",
volume = "73",
pages = "40--46",
journal = "Bioscience, Biotechnology and Biochemistry",
issn = "0916-8451",
publisher = "Japan Society for Bioscience Biotechnology and Agrochemistry",
number = "1",
}