Uçarlı Cüneyt, McGuffin Liam J, Çaputlu Süleyman, Aravena Andres, Gürel Filiz
Department of Molecular Biology and Genetics, Faculty of Science, Istanbul University, Vezneciler 34134, Istanbul, Turkey.
School of Biological Sciences, University of Reading, Whiteknights, Reading RG6 6AS, UK.
Sci Rep. 2016 Feb 12;6:20966. doi: 10.1038/srep20966.
We analysed Hordeum spontaneum accessions from 21 different locations to understand the genetic diversity of HsDhn3 alleles and effects of single base mutations on the intrinsically disordered structure of the resulting polypeptide (HsDHN3). HsDHN3 was found to be YSK2-type with a low-frequency 6-aa deletion in the beginning of Exon 1. There is relatively high diversity in the intron region of HsDhn3 compared to the two exon regions. We have found subtle differences in K segments led to changes in amino acids chemical properties. Predictions for protein interaction profiles suggest the presence of a protein-binding site in HsDHN3 that coincides with the K1 segment. Comparison of DHN3 to closely related cereals showed that all of them contain a nuclear localization signal sequence flanking to the K1 segment and a novel conserved region located between the S and K1 segments [E(D/T)DGMGGR]. We found that H. vulgare, H. spontaneum, and Triticum urartu DHN3s have a greater number of phosphorylation sites for protein kinase C than other cereal species, which may be related to stress adaptation. Our results show that the nature and extent of mutations in the conserved segments of K1 and K2 are likely to be key factors in protection of cells.
我们分析了来自21个不同地点的野生大麦种质,以了解HsDhn3等位基因的遗传多样性以及单碱基突变对所得多肽(HsDHN3)内在无序结构的影响。发现HsDHN3为YSK2型,在外显子1开头有一个低频的6个氨基酸缺失。与两个外显子区域相比,HsDhn3的内含子区域具有相对较高的多样性。我们发现K段的细微差异导致了氨基酸化学性质的变化。蛋白质相互作用图谱预测表明,HsDHN3中存在一个与K1段重合的蛋白质结合位点。将DHN3与近缘谷类进行比较表明,它们都含有一个位于K1段侧翼的核定位信号序列以及一个位于S段和K1段之间的新保守区域[E(D/T)DGMGGR]。我们发现,与其他谷类物种相比,大麦、野生大麦和乌拉尔图小麦的DHN3具有更多的蛋白激酶C磷酸化位点,这可能与胁迫适应有关。我们的结果表明,K1和K2保守段中突变的性质和程度可能是保护细胞的关键因素。