Characterization and biological function analysis of the trim3a gene from zebrafish (Danio rerio)

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• 作者：Xinshang Zhang^a ; Heng Zhao^a ; ^{hengzhao2000@gmail.com} ; Yeyu Chen^a ; Chao Liu^b ; Kun Meng^a ; Peilong Yang^a ; Yaru Wang^a ; Guozeng Wang^a ; Bin Yao^a ; ^{binyao@caas.net.cn} ; ^{yaobin@mail.caas.net.cn}
• 关键词：TRIM3a ; Tissue distribution ; E3 ubiquitin ligase
• 刊名：Fish & Shellfish Immunology
• 出版年：2012
• 期刊代码：115_10504648
• 类别：abs
• 出版时间：May, 2012
• 卷：32
• 期：5
• 页码：621-628
• 文件大小：821 K

摘要

The biological significance of tripartite motif (TRIM) proteins is increasingly being appreciated due to their roles in a broad range of biological processes that associated with innate immunity. In this study, we have described the structural and functional analysis of TRIM3a from zebrafish. Annotation of domain architectures found that the TRIM3a fulfills the TRIM-NHL rule of domain composition with a Filamin/ABP280 domain and NHL repeats at its C-terminal region. In addition, the mRNA expression level of TRIM3a was the highest in brain, and with a relatively higher level in spleen, liver, and gill. A strong expression starting at 36聽h post fertilization (hpf) was observed by real-time PCR and could be detected in brain by m>in situ hybridizationm>, suggesting that TRIM3a protein might play an important role in brain development in zebrafish. Considering that TRIM3a has a RING finger domain, we expressed and purified the TRIM3a protein and performed ubiquitylation assays, our results showed that TRIM3a underwent self-polyubiquitylation in combination with E1, UbcH5c, biotin-ubiquitin m>in聽vitrom>. Meanwhile, TRIM3a-R without the RING domain was expressed and purified as well, m>in聽vitrom> ubiquitylation assays showed that the self-ubiquitylation of TRIM3a was dependent on its RING domain, suggesting that TRIM3a might function as a RING finger E3 ubiquitin ligase.