The Dysferlin Domain-Only Protein, Spo73, Is Required for Prospore Membrane Extension in Saccharomyces cerevisiae

Author:

Okumura Yuuya1,Nakamura Tsuyoshi S.1,Tanaka Takayuki1,Inoue Ichiro1,Suda Yasuyuki2,Takahashi Tetsuo3,Nakanishi Hideki4,Nakamura Shugo5,Gao Xiao-Dong4,Tachikawa Hiroyuki1

Affiliation:

1. Department of Applied Biological Chemistry, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan

2. Department of Molecular Cell Biology, Graduate School of Comprehensive Human Sciences and Institute of Basic Medical Sciences, University of Tsukuba, Tsukuba, Japan

3. Laboratory of Glycobiology and Glycotechnology, Department of Applied Biochemistry, School of Engineering, Tokai University, Hiratsuka City, Kanagawa, Japan

4. Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi, China

5. Department of Biotechnology, Graduate School of Agricultural and Life Sciences, The University of Tokyo, Bunkyo-ku, Tokyo, Japan

Abstract

Prospore membrane formation consists of de novo double-membrane formation, which occurs during the developmental process of sporulation in Saccharomyces cerevisiae . Membranes are formed into their proper size and shape, and thus, prospore membrane formation has been studied as a general model of membrane formation. We identified SPO73 , previously shown to be required for spore wall formation, as an additional gene involved in prospore membrane extension. Genetic and cell biological analyses suggested that Spo73 functions on the prospore membrane with other factors in prospore membrane extension, counteracting the bending force of the prospore membrane. Spo73 is the first dysferlin domain-only protein ever analyzed. The dysferlin domain is conserved from yeast to mammals and is found in dysferlin proteins, which are involved in dysferlinopathy, although the precise function of the domain is unknown. Continued analysis of Spo73 will contribute to our understanding of the function of dysferlin domains and dysferlinopathy.

Funder

Japan Society for the Promotion of Science

Toujuro Iijima Foundation for Food Science and Technology

Publisher

American Society for Microbiology

Subject

Molecular Biology,Microbiology

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