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通过实验和计算方法对果蝇中作为14 kDa硫氧还蛋白相关蛋白的Clot进行基于结构的分析。

Structure-based analysis of Clot as a thioredoxin-related protein of 14 kDa in Drosophila via experimental and computational approaches.

作者信息

Kim Kiyoung

机构信息

Department of Medical Biotechnology, Soonchunhyang University, Asan, 31538, Korea.

出版信息

Biotechnol Appl Biochem. 2018 May;65(3):338-345. doi: 10.1002/bab.1624. Epub 2017 Nov 15.

DOI:10.1002/bab.1624
PMID:29080217
Abstract

The clot gene is required for the biosynthesis of drosopterins, the red components of Drosophila eye pigments. However, the enzymatic role of Clot in Drosophila eye pigment formation and the molecular mechanisms underlying Clot function are not fully elucidated. In this study, we cloned and characterized Clot derived from Drosophila cDNA, and results showed that Clot exhibited ∼30% sequence identity with mammalian TRP14. In addition, we reported the three-dimensional structure of Drosophila Clot based on homology modeling. Furthermore, we identified NFκB as a novel Clot substrate using the I-TASSER program. The NFκB fragment can bind near the active site of Clot. These findings predicted the novel regulatory mechanisms underlying Clot function in the pyrimidodiazepine synthesis pathway and increased the understanding of the molecular mechanisms and physiological function of Clot in Drosophila eye pigment formation.

摘要

凝块基因是果蝇蝶呤生物合成所必需的,果蝇蝶呤是果蝇眼色素的红色成分。然而,凝块在果蝇眼色素形成中的酶促作用以及凝块功能的分子机制尚未完全阐明。在本研究中,我们克隆并鉴定了源自果蝇cDNA的凝块,结果表明凝块与哺乳动物TRP14具有约30%的序列同一性。此外,我们基于同源建模报道了果蝇凝块的三维结构。此外,我们使用I-TASSER程序鉴定出NFκB是一种新的凝块底物。NFκB片段可以结合在凝块活性位点附近。这些发现预测了凝块在嘧啶二氮杂卓合成途径中功能的新调控机制,并增进了对凝块在果蝇眼色素形成中的分子机制和生理功能的理解。

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