Predicting conserved domain and structural variations of prenyl transferase sequence variants in Triticum urartu

2016 International Conference on Bioinformatics and Systems Biology (BSB) Pub Date : 2016-03-04 DOI:10.1109/BSB.2016.7552155

Mamta Sagar, P. Ramteke, Arvind Kumar Yadav

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Abstract

Prenyl transferase enzyme is widely distributed among plants. This enzyme catalyses prenylation reaction, that leads to increased flavonoid's activity. In this research, highly conserved polyprenyl patterns have been analysed in plants. Prenyl transferase in Triticum urartu, Oryza sativa japonica and Zea mays share presence of conserved motif LIhDDviDdsgmRRG. This protein share the presence of motif LVlDDimDnsqtRRG in Lupinus albus and Phaseolus vulgaris, both motifs belong to polyprenyl signature 1. Prenyl transferase of Triticum urartu do not contain polyprenyl signature 2. Here, polyprenyl signature 2 motif has been inserted into the protein of Triticum urartu at 273 position, which was extracted from above plants. Structural variations have been analysed using homology modelling after insertion of LGlsFQVvDDIlD and MGtyFQVqDDYlD motifs into protein of Triticum urartu. Modifications in protein do not show any unfavourable changes or disruption in structure. Analysis of Conserved domain Trans-Isoprenyl Diphosphate Synthases shows presence of enhanced substrate binding pocket, catalytic residues in modified Prenyl Transferase.

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乌拉尔小麦戊烯基转移酶序列变异的保守域和结构变异预测

戊烯基转移酶广泛分布于植物中。这种酶催化烯酰化反应，导致类黄酮活性增加。本研究分析了植物中高度保守的聚戊烯基结构。小麦、粳稻和玉米的戊烯基转移酶可能共享保守基序LIhDDviDdsgmRRG。该蛋白在白Lupinus albus和Phaseolus vulgaris中均存在LVlDDimDnsqtRRG基序，均属于聚戊烯基特征1。乌拉尔小麦的戊烯基转移酶不含聚戊烯基特征2。本文将聚戊烯基标记2基序插入到从上述植物中提取的乌拉尔小麦蛋白的第273位。将lglsfqvvddld和MGtyFQVqDDYlD基序插入乌拉尔小麦蛋白后，利用同源性模型分析其结构变化。蛋白质的修饰不会显示出任何不利的变化或结构的破坏。对保守结构域反式异戊烯基二磷酸合酶的分析表明，在修饰的戊烯基转移酶中存在增强的底物结合袋和催化残基。

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2016 International Conference on Bioinformatics and Systems Biology (BSB)

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