Chemical shift assignment of a thermophile frataxin.
Chemical shift assignment of a thermophile frataxin.
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DOI：
10.1007/s12104-017-9790-3
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发表时间：
2018-04
影响因子：
0.9
通讯作者：
Pastore A
中科院分区：
文献类型：
--
作者：
Rasheed M;Yan R;Kelly G;Pastore A
Frataxin是负责遗传性神经退行性疾病Friedreich共济失调的蛋白质，该疾病由蛋白质的部分沉默和功能丧失引起。尽管frataxin的功能还不完全清楚，但它与构建铁硫簇的机器有关，铁硫簇是参与几个过程的重要辅基，并且在从细菌到人类的生物体中高度保守。它的两个重要分子伴侣是蛋白质NFS1（或细菌中的IscS），即将半胱氨酸转化为丙氨酸并产生硫的脱硫酶，以及ISU（或IscU），瞬时接受簇的支架蛋白。虽然细菌共济失调蛋白已被广泛表征，但只有少数真核共济失调蛋白被描述。在这里，我们报告的1H，13 C和15 N的骨干和侧链化学位移分配frataxin从嗜热毛壳菌，嗜热越来越多地使用凭借其稳定性。
Frataxin is the protein responsible for the genetically-inherited neurodegenerative disease Friedreich’s ataxia caused by partial silencing of the protein and loss of function. Although the frataxin function is not yet entirely clear, it has been associated to the machine that builds iron–sulfur clusters, essential prosthetic groups involved in several processes and is strongly conserved in organisms from bacteria to humans. Two of its important molecular partners are the protein NFS1 (or IscS in bacteria), that is the desulfurase which converts cysteine to alanine and produces sulfur, and ISU (or IscU), the scaffold protein which transiently accepts the cluster. While bacterial frataxin has been extensively characterized, only few eukaryotic frataxins have been described. Here we report the 1H, 13C and 15N backbone and side-chain chemical shift assignments of frataxin from Chaetomium thermophilum, a thermophile increasingly used by virtue of its stability.
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影响因子：
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期刊：
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