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A Glycosylphosphatidylinositol-Anchored α-Amylase Encoded by amyD Contributes to a Decrease in the Molecular Mass of Cell Wall α-1,3-Glucan in Aspergillus nidulans

Authors :
Ken Miyazawa
Takaaki Yamashita
Ayumu Takeuchi
Yuka Kamachi
Akira Yoshimi
Yuto Tashiro
Ami Koizumi
Makoto Ogata
Shigekazu Yano
Shin Kasahara
Motoaki Sano
Youhei Yamagata
Tasuku Nakajima
Keietsu Abe
Source :
Frontiers in Fungal Biology, Vol 2 (2022)
Publication Year :
2022
Publisher :
Frontiers Media SA, 2022.

Abstract

α-1,3-Glucan is one of the main polysaccharides in the cell wall of Aspergillus nidulans. We previously revealed that it plays a role in hyphal aggregation in liquid culture, and that its molecular mass (MM) in an agsA-overexpressing (agsAOE) strain was larger than that in an agsB-overexpressing (agsBOE) strain. The mechanism that regulates its MM is poorly understood. Although the gene amyD, which encodes glycosylphosphatidylinositol (GPI)-anchored α-amylase (AmyD), is involved in the biosynthesis of α-1,3-glucan in A. nidulans, how it regulates this biosynthesis remains unclear. Here we constructed strains with disrupted amyD (ΔamyD) or overexpressed amyD (amyDOE) in the genetic background of the ABPU1 (wild-type), agsAOE, or agsBOE strain, and characterized the chemical structure of α-1,3-glucans in the cell wall of each strain, focusing on their MM. The MM of α-1,3-glucan from the agsBOEamyDOE strain was smaller than that in the parental agsBOE strain. In addition, the MM of α-1,3-glucan from the agsAOE ΔamyD strain was greater than that in the agsAOE strain. These results suggest that AmyD is involved in decreasing the MM of α-1,3-glucan. We also found that the C-terminal GPI-anchoring region is important for these functions.

Details

ISSN :
26736128
Volume :
2
Database :
OpenAIRE
Journal :
Frontiers in Fungal Biology
Accession number :
edsair.doi.dedup.....16aa0c81a61ce42c5d0941f2179ef4dd
Full Text :
https://doi.org/10.3389/ffunb.2021.821946