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Atg22p,一种参与粟酒裂殖酵母氨基酸区室化的液泡膜蛋白。

Atg22p, a vacuolar membrane protein involved in the amino acid compartmentalization of Schizosaccharomyces pombe.

作者信息

Sugimoto Naoko, Iwaki Tomoko, Chardwiriyapreecha Soracom, Shimazu Masamitsu, Kawano Miyuki, Sekito Takayuki, Takegawa Kaoru, Kakinuma Yoshimi

机构信息

Department of Applied Bioresource Science, Faculty of Agriculture, Ehime University, Matsuyama, Japan.

出版信息

Biosci Biotechnol Biochem. 2011;75(2):385-7. doi: 10.1271/bbb.100747. Epub 2011 Feb 7.

Abstract

The fission yeast Schizosaccharomyces pombe has a homolog of the budding yeast Atg22p, which is involved in spore formation (Mukaiyama H. et al., Microbiology, 155, 3816-3826 (2009)). GFP-tagged Atg22p in the fission yeast was localized to the vacuolar membrane. Upon disruption of atg22, the amino acid levels of the cellular fraction as well as the vacuolar fraction decreased. The uptake of several amino acids, such as lysine, histidine, and arginine, was impaired in atg22Δ cells. S. pombe Atg22p plays an important role in the compartmentalization of amino acids.

摘要

裂殖酵母粟酒裂殖酵母有芽殖酵母Atg22p的同源物,其参与孢子形成(Mukaiyama H.等人,《微生物学》,155,3816 - 3826(2009))。裂殖酵母中绿色荧光蛋白标记的Atg22p定位于液泡膜。atg22破坏后,细胞组分以及液泡组分的氨基酸水平降低。atg22Δ细胞中赖氨酸、组氨酸和精氨酸等几种氨基酸的摄取受损。粟酒裂殖酵母Atg22p在氨基酸的区室化中起重要作用。

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