Distinct catalytic capacities of two aluminium-repressed Arabidopsis thaliana xyloglucan endotransglucosylase/hydrolases, XTH15 and XTH31, heterologously produced in Pichia

文献类型： 外文期刊

第一作者： Shi, Yuan Zhi

作者： Shi, Yuan Zhi;Zhu, Xiao Fang;Zheng, Shao Jian;Shi, Yuan Zhi;Miller, Janice G.;Gregson, Timothy;Fry, Stephen C.;Shi, Yuan Zhi

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关键词： Arabidopsis thaliana;XTH15;XTH31;Plant cell wall;Xyloglucan;XET;XEH;Acid growth

期刊名称：PHYTOCHEMISTRY （ 影响因子：4.072； 五年影响因子：4.132 ）

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收录情况： SCI

摘要： Xyloglucan plays an important structural role in primary cell walls, possibly tethering adjacent microfibrils and restraining cell expansion. There is therefore considerable interest in understanding the role of xyloglucan endotransglucosylase/hydrolases (XTHs), which are encoded in Arabidopsis by a 33-member gene family. We compared the key catalytic properties of two very different Arabidopsis XTHs (heterologously produced in Pichia), both of which are aluminium-repressed. Reductively tritiated oligosaccharides of xyloglucan were used as model acceptor substrates. Untransformed Pichia produced no xyloglucan-acting enzymes; therefore purification of the XTHs was unnecessary. XTH15, a classical group-I/II XTH, had high XET and undetectable XEH activity in vitro; its XET K-m values were 31 mu M XXXGol (acceptor substrate) and 2.9 mg/ml xyloglucan (donor substrate). In contrast, XTH31, a group-III-A XTH, showed predominant XEH activity and only slight XET activity in vitro; its XET K-m was 86 mu M XXXGol (acceptor), indicating a low affinity of this predominantly hydrolytic protein for a transglycosylation acceptor substrate. The K-m of XTH31's XEH activity was 1.6 mg/ml xyloglucan. For both proteins, the preferred XET acceptor substrate, among five cellotetraitol-based oligosaccharides tested, was XXXGol. XTH31's XET activity was strongly compromised when the second Xyl residue was galactosylated. XTH15's XET activity, in contrast, tolerated substitution at the second Xyl residue. The two enzymes also showed different pH preferences, XTH31 exhibiting an unusually low pH optimum and XTH15 an unusually broad optimum. XTH31's hydrolase activity increased almost linearly with decreasing pH in the apoplastic range, 6.2-4.5, consistent with a possible role in 'acid growth'. In conclusion, these two Al3+-repressed XTHs differ, in several important enzymic features, from other members of the Arabidopsis XTH family. (C) 2014 Elsevier Ltd. All rights reserved.

分类号： Q94

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