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The effect of salt and temperature on the conformational changes of P1LEA‐22, a repeat unit of plant Late Embryogenesis Abundant proteins
Journal of Peptide Science ( IF 1.8 ) Pub Date : 2020-03-11 , DOI: 10.1002/psc.3247
David Léon 1 , Michael P. Vermeuel 1 , Priya Gupta 1 , Michelle R. Bunagan 1
Affiliation  

The effect of choline chloride on the conformational dynamics of the 11‐mer repeat unit P1LEA‐22 of group 3 Late Embryogenesis Abundant (G3LEA) proteins was studied. Circular dichroism data of aqueous solutions of P1LEA‐22 revealed that the peptide favors a polyproline II (PPII) helix structure at low temperature, with increasing temperature promoting a gain of unstructured conformations. Furthermore, increases in sample FeCl3 or choline chloride concentrations causes a gain in PPII helical structure at low temperature. The potential role of PPII structure in intrinsically disordered and G3LEA proteins is discussed, including its ability to easily access other secondary structural conformations such as α‐helix and β‐sheet, which have been observed for dehydrated G3LEA proteins. The observed effect of FeCl3 and choline chloride salts on P1LEA‐22 suggests favorable cation interactions with the PPII helix, supporting ion sequestration as a G3LEA protein function. As choline chloride is suggested to improve salt tolerance and protect cell membrane in plants at low temperature, our results support adoption of the PPII structure as a possible damage‐preventing measure of Late Embryogenesis Abundant proteins.

中文翻译:

盐和温度对植物晚期胚胎发生的重复单元P1LEA-22构象变化的影响

研究了氯化胆碱对第3组晚期胚胎发生丰富(G3LEA)蛋白的11-mer重复单元P1LEA-22构象动力学的影响。P1LEA-22水溶液的圆二色性数据显示,该肽在低温下有利于聚脯氨酸II(PPII)螺旋结构,随着温度的升高,促进了非结构化构象的获得。此外,样品FeCl 3或氯化胆碱浓度的增加导致低温下PPII螺旋​​结构的增加。讨论了PPII结构在本质上无序的G3LEA蛋白中的潜在作用,包括其易于访问其他二级结构构象(如α-螺旋和β-sheet)的能力,这些构象已在脱水的G3LEA蛋白中观察到。FeCl的观察效果3和P1LEA-22上的胆碱盐酸盐表明与PPII螺旋​​具有良好的阳离子相互作用,支持离子螯合作为G3LEA蛋白功能。由于建议使用氯化胆碱来提高植物的耐盐性并在低温下保护植物的细胞膜,因此我们的研究结果支持采用PPII结构作为可能的预防晚期胚胎发生的蛋白质过多的措施。
更新日期:2020-03-11
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