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A SNP in the 3 '-UTR of HSF1 in dairy cattle affects binding of target bta-miR-484

文献类型： 外文期刊

作者： Li, Q. L. 1 ; Zhang, Z. F. 2 ; Xia, P. 1 ; Wang, Y. J. 1 ; Wu, Z. Y. 1 ; Jia, Y. H. 1 ; Chang, S. M. 1 ; Chu, M. X. 4 ;

作者机构： 1.Langfang Teachers Univ, Edible & Med Fungi Res & Dev Ctr, Coll Life Sci, Langfang, Peoples R China

2.Langfang Agr Bur, Vet Adm Off, Langfang, Peoples R China

3.Shandong Acad Agr Sci, Dairy Cattle Res Ctr, Jinan, Peoples R China

4.Chinese Acad Agr Sci, Inst Anim Sci, Minist Agr, Key Lab Farm Anim Genet Resources & Germplasm Inn, Beijing 100193, Peoples R China

关键词： Dairy cattle;HSF1;bta-miR-484;Thermo tolerance;Target;Single nucleotide polymorphism

期刊名称：GENETICS AND MOLECULAR RESEARCH （ 影响因子：0.764； 五年影响因子：0.912 ）

ISSN： 1676-5680

年卷期： 2015 年 14 卷 4 期

页码：

收录情况： SCI

摘要： The heat shock transcription factor 1 gene (HSF1) plays a key role in the heat stress response. We previously found a single nucleotide polymorphism (SNP) in the 3'-untranslated region (g.4693G>T) of HSF1 that was related to thermo tolerance in Chinese Holstein cattle through association analysis. However, it is not known whether other SNPs also affect thermo tolerance. In this study a novel SNP, g.1451G>T, was identified by DNA sequencing and genotyped using creating restriction site-polymerase chain reaction methodology. The g.1451G>T polymorphic site met Hardy-Weinberg equilibrium (P > 0.05). Association analysis demonstrated that this SNP had no effect on thermo tolerance traits in Holstein cattle. Findings of the study compared to the analysis of g.4693G>T further indicated that g.4693 G>T may play an important role in thermo tolerance, although the mechanism is not clear. RNA hybrid and Targetscan prediction showed that the minimum free energy hybridization of bta-miR-484 with HSF1 3'-UTR was -31.9 kcal/mol and g.4693 G>T was in the seed sequence of bovine HSF1 that binds to bta-miR-484. Analysis by Luciferase assay indicated that HSF1 expression was directly targeted by bta-miR-484 in HEK 293T cells, and the Rluc/luc ratio of wildtype (GG) was lower than that of the mutant (TT) (P < 0.05). These results suggest that g.4693 G>T affects binding of HSF1 to bta-miR-484.

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