NMR assignments of the WBSCR27 protein related to Williams-Beuren syndrome

被引:3
|
作者
Mariasina, Sofia S. [1 ,2 ]
Petrova, Olga A. [3 ]
Osterman, Ilya A. [2 ,3 ,4 ]
Sergeeva, Olga V. [4 ]
Efimov, Sergey V. [5 ]
Klochkov, Vladimir V. [5 ]
Sergiev, Petr V. [2 ,3 ,4 ]
Dontsova, Olga A. [2 ,3 ,4 ]
Huang, Tai-huang [6 ]
Chang, Chi-Fon [7 ]
Polshakov, Vladimir I. [1 ]
机构
[1] Moscow MV Lomonosov State Univ, Fac Fundamental Med, Ctr Magnet Tomog & Spect, Moscow 119991, Russia
[2] Moscow MV Lomonosov State Univ, Dept Chem, Moscow 119991, Russia
[3] Moscow MV Lomonosov State Univ, AN Belozersky Inst Physicochem Biol, Moscow 119991, Russia
[4] Skolkovo Inst Sci & Technol, Moscow, Russia
[5] Kazan Fed Univ, Inst Phys, NMR Lab, 18 Kremlevskaya, Kazan 420008, Russia
[6] Acad Sinica, Inst Biomed Sci, Taipei, Taiwan
[7] Acad Sinica, Genom Res Ctr, Taipei, Taiwan
基金
俄罗斯科学基金会; 俄罗斯基础研究基金会;
关键词
SAM-dependent methyltransferases; Williams-Beuren syndrome; Protein NMR; Resonance assignment; Secondary structure; 18S RIBOSOMAL-RNA; METHYLATION; DISORDER;
D O I
10.1007/s12104-018-9827-2
中图分类号
Q6 [生物物理学];
学科分类号
071011 ;
摘要
Williams-Beuren syndrome is a genetic disorder characterized by physiological and mental abnormalities, and is caused by hemizygous deletion of several genes in chromosome 7. One of the removed genes encodes the WBSCR27 protein. Bioinformatic analysis of the sequence of WBSCR27 indicates that it belongs to the family of SAM-dependent methyltransferases. However, exact cellular functions of this protein or phenotypic consequences of its deficiency are still unknown. Here we report nearly complete H-1, N-15, and C-13 chemical shifts assignments of the 26kDa WBSCR27 protein from Mus musculus in complex with the cofactor S-adenosyl-l-methionine (SAM). Analysis of the assigned chemical shifts allowed us to characterize the protein's secondary structure and backbone dynamics. The topology of the protein's fold confirms the assumption that the WBSCR27 protein belongs to the family of class I methyltransferases.
引用
收藏
页码:303 / 308
页数:6
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