耐热链霉菌HF3-3 α-1,3-葡聚糖酶结构域的功能分析

IF 0.8 4区 生物学 Q4 BIOTECHNOLOGY & APPLIED MICROBIOLOGY Journal of General and Applied Microbiology Pub Date : 2021-07-31 Epub Date: 2021-02-12 DOI:10.2323/jgam.2020.07.003
Niphawan Panti, Vipavee Cherdvorapong, Takafumi Itoh, Takao Hibi, Wassana Suyotha, Shigekazu Yano, Mamoru Wakayama
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引用次数: 0

摘要

耐热链霉菌HF3-3 (Agl-ST) α-1,3-葡聚糖酶属于糖苷水解酶(GH)家族87。Agl-ST是一个多模块结构域,由n端β-三明治结构域(β-SW)、催化结构域(UC)和c端盘状蛋白结构域(DS)组成。虽然Agl-ST不水解α-1,4-糖苷键,但其氨基酸序列更接近GH87真菌葡聚糖酶而不是α-1,3-葡聚糖酶。它可能被归类为GH87的一个新亚家族。在这项研究中,我们研究了结构域的功能。构建了多个结构域与绿色荧光蛋白(GFP)的融合蛋白,以明确每个结构域的功能。结果表明,β-SW和DS结构域结合α-1,3-葡聚糖,促进α-1,3-葡聚糖的水解。结合域β-SW和DS对木聚糖也表现出结合活性,但对α-1,3-葡聚糖的结合活性较低。β-SW和DS结构域的结合表明Agl-ST对α-1,3-葡聚糖具有较高的结合和水解活性,而催化结构域仅具有催化功能。结合结构域还能有效结合和水解裂叶菌细胞壁复合物中的α-1,3-葡聚糖。
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Functional analysis of α-1,3-glucanase domain structure from Streptomyces thermodiastaticus HF3-3.

α-1,3-Glucanase from Streptomyces thermodiastaticus HF3-3 (Agl-ST) has been classified in the glycoside hydrolase (GH) family 87. Agl-ST is a multi-modular domain consisting of an N-terminal β-sandwich domain (β-SW), a catalytic domain, an uncharacterized domain (UC), and a C-terminal discoidin domain (DS). Although Agl-ST did not hydrolyze α-1,4-glycosidic bonds, its amino acid sequence is more similar to GH87 mycodextranase than to α-1,3-glucanase. It might be categorized into a new subfamily of GH87. In this study, we investigated the function of the domains. Several fusion proteins of domains with green fluorescence protein (GFP) were constructed to clarify the function of each domain. The results showed that β-SW and DS domains played a role in binding α-1,3-glucan and enhancing the hydrolysis of α-1,3-glucan. The binding domains, β-SW and DS, also showed binding activity toward xylan, although it was lower than that for α-1,3-glucan. The combination of β-SW and DS domains demonstrated high binding and hydrolysis activities of Agl-ST toward α-1,3-glucan, whereas the catalytic domain showed only a catalytic function. The binding domains also achieved effective binding and hydrolysis of α-1,3-glucan in the cell wall complex of Schizophyllum commune.

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来源期刊
Journal of General and Applied Microbiology
Journal of General and Applied Microbiology 生物-生物工程与应用微生物
CiteScore
2.40
自引率
0.00%
发文量
42
审稿时长
6-12 weeks
期刊介绍: JGAM is going to publish scientific reports containing novel and significant microbiological findings, which are mainly devoted to the following categories: Antibiotics and Secondary Metabolites; Biotechnology and Metabolic Engineering; Developmental Microbiology; Environmental Microbiology and Bioremediation; Enzymology; Eukaryotic Microbiology; Evolution and Phylogenetics; Genome Integrity and Plasticity; Microalgae and Photosynthesis; Microbiology for Food; Molecular Genetics; Physiology and Cell Surface; Synthetic and Systems Microbiology.
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