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首页> 外文期刊>Acta crystallographica, Section F. Structural biology and crystallization communications >Overexpression, crystallization and preliminary X-ray crystallographic analysis of release factor eRF1-1 from Arabidopsis thaliana
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Overexpression, crystallization and preliminary X-ray crystallographic analysis of release factor eRF1-1 from Arabidopsis thaliana

机译：拟南芥释放因子eRF1-1的过表达，结晶和初步X射线晶体学分析

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摘要

Peptide release factor 1 (RF1) regulates the termination of translation in protein synthesis by recognizing the stop codons. The eukaryotic RF1s (eRF1s) from Arabidopsis thaliana and human have different stop-codon preferences even though they share high sequence similarity. Based on known RF1 structures, it has been suggested that the specificity depends on both the local structure and the domain arrangement, but the lack of a structure of Arabidopsis eRF1 hinders a detailed comparison. To reveal the mechanism of stop-codon recognition and compare it with that of human eRF1, one of the three Arabidopsis eRF1s, AteRF1-1, was studied and a preliminary X-ray crystallographic analysis is reported here. The protein was overexpressed in Escherichia coli and crystallized at room temperature using the vapour-diffusion method. Crystals were grown from 1.6 M lithium sulfate, 0.1 M Tris-HCl pH 8.0, 2%(v/v) PEG 400 and diffracted to 3.77 angstrom resolution. The data were processed in point group 622, with unit-cell parameters a = b = 136.6, c = 325.7 angstrom.
机译：肽释放因子1（RF1）通过识别终止密码子来调节蛋白质合成中翻译的终止。尽管拟南芥和人类的真核RF1（eRF1s）具有很高的序列相似性，但它们具有不同的终止密码子偏好。基于已知的RF1结构，已经提出特异性取决于局部结构和结构域排列，但是缺乏拟南芥eRF1的结构阻碍了详细的比较。为了揭示终止密码子识别的机理并将其与人类eRF1进行比较，研究了三种拟南芥eRF1之一AteRF1-1，并在此报道了初步的X射线晶体学分析。该蛋白质在大肠杆菌中过表达，并在室温下使用蒸气扩散法结晶。晶体从1.6 M硫酸锂，0.1 M Tris-HCl pH 8.0、2％（v / v）PEG 400生长，并衍射至3.77埃分辨率。数据在点组622中处理，单位像元参数a = b = 136.6，c = 325.7埃。

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