Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall

The surface of the <i>Saccharomyces cerevisiae</i> spore wall exhibits a ridged appearance. The outermost layer of the spore wall is believed to be a dityrosine layer, which is primarily composed of a crosslinked dipeptide bisformyl dityrosine. The dityrosine layer is impervious to prote...

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Main Authors: Yan Yang, Ganglong Yang, Zi-Jie Li, Yi-Shi Liu, Xiao-Dong Gao, Hideki Nakanishi
Format: Article
Language:English
Published: MDPI AG 2023-03-01
Series:Journal of Fungi
Subjects:
Online Access:https://www.mdpi.com/2309-608X/9/4/392
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author Yan Yang
Ganglong Yang
Zi-Jie Li
Yi-Shi Liu
Xiao-Dong Gao
Hideki Nakanishi
author_facet Yan Yang
Ganglong Yang
Zi-Jie Li
Yi-Shi Liu
Xiao-Dong Gao
Hideki Nakanishi
author_sort Yan Yang
collection DOAJ
description The surface of the <i>Saccharomyces cerevisiae</i> spore wall exhibits a ridged appearance. The outermost layer of the spore wall is believed to be a dityrosine layer, which is primarily composed of a crosslinked dipeptide bisformyl dityrosine. The dityrosine layer is impervious to protease digestion; indeed, most of bisformyl dityrosine molecules remain in the spore after protease treatment. However, we find that the ridged structure is removed by protease treatment. Thus, a ridged structure is distinct from the dityrosine layer. By proteomic analysis of the spore wall-bound proteins, we found that hydrophilin proteins, including Sip18, its paralog Gre1, and Hsp12, are present in the spore wall. Mutant spores with defective hydrophilin genes exhibit functional and morphological defects in their spore wall, indicating that hydrophilin proteins are required for the proper organization of the ridged and proteinaceous structure. Previously, we found that RNA fragments were attached to the spore wall in a manner dependent on spore wall-bound proteins. Thus, the ridged structure also accommodates RNA fragments. Spore wall-bound RNA molecules function to protect spores from environmental stresses.
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spelling doaj.art-b85c1de7bbc647038024ed3ce3de967b2023-11-17T19:57:30ZengMDPI AGJournal of Fungi2309-608X2023-03-019439210.3390/jof9040392Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore WallYan Yang0Ganglong Yang1Zi-Jie Li2Yi-Shi Liu3Xiao-Dong Gao4Hideki Nakanishi5Key Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, ChinaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaState Key Laboratory of Biochemical Engineering, Institute of Process Engineering, Chinese Academy of Sciences, Beijing 100190, ChinaKey Laboratory of Carbohydrate Chemistry and Biotechnology, Ministry of Education, School of Biotechnology, Jiangnan University, Wuxi 214122, ChinaThe surface of the <i>Saccharomyces cerevisiae</i> spore wall exhibits a ridged appearance. The outermost layer of the spore wall is believed to be a dityrosine layer, which is primarily composed of a crosslinked dipeptide bisformyl dityrosine. The dityrosine layer is impervious to protease digestion; indeed, most of bisformyl dityrosine molecules remain in the spore after protease treatment. However, we find that the ridged structure is removed by protease treatment. Thus, a ridged structure is distinct from the dityrosine layer. By proteomic analysis of the spore wall-bound proteins, we found that hydrophilin proteins, including Sip18, its paralog Gre1, and Hsp12, are present in the spore wall. Mutant spores with defective hydrophilin genes exhibit functional and morphological defects in their spore wall, indicating that hydrophilin proteins are required for the proper organization of the ridged and proteinaceous structure. Previously, we found that RNA fragments were attached to the spore wall in a manner dependent on spore wall-bound proteins. Thus, the ridged structure also accommodates RNA fragments. Spore wall-bound RNA molecules function to protect spores from environmental stresses.https://www.mdpi.com/2309-608X/9/4/392<i>Saccharomyces cerevisiae</i>sporecell wallhydrophilinRNA
spellingShingle Yan Yang
Ganglong Yang
Zi-Jie Li
Yi-Shi Liu
Xiao-Dong Gao
Hideki Nakanishi
Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
Journal of Fungi
<i>Saccharomyces cerevisiae</i>
spore
cell wall
hydrophilin
RNA
title Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
title_full Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
title_fullStr Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
title_full_unstemmed Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
title_short Studies on the Proteinaceous Structure Present on the Surface of the <i>Saccharomyces cerevisiae</i> Spore Wall
title_sort studies on the proteinaceous structure present on the surface of the i saccharomyces cerevisiae i spore wall
topic <i>Saccharomyces cerevisiae</i>
spore
cell wall
hydrophilin
RNA
url https://www.mdpi.com/2309-608X/9/4/392
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