Open Access
Open access
Frontiers in Molecular Biosciences, том 9

Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function

Chang Chi-Fon 3
Navalayeu Tsimafei L 4
Chugunova Anastasia A 4
Efimov Sergey V 5
Zgoda Viktor G 6
Ivlev Vasily A 7
Dontsova Olga A. 4, 8
Sergiev Petr V. 2, 4, 8
Faculty of Fundamental Medicine, Russia
Institute of Functional Genomics, Russia
Genomics Research Center, Taiwan
Chemical Department, Russia
NMR Laboratory, Russia
Тип документаJournal Article
Дата публикации2022-06-15
Frontiers Media S.A.
Frontiers Media S.A.
Название журналаFrontiers in Molecular Biosciences
Квартиль по SCImago1
Квартиль по Web of Science
Импакт-фактор 20216.11
Molecular Biology
Biochemistry, Genetics and Molecular Biology (miscellaneous)
Краткое описание

Williams-Beuren syndrome (WBS) is a genetic disorder associated with the hemizygous deletion of several genes in chromosome 7, encoding 26 proteins. Malfunction of these proteins induce multisystemic failure in an organism. While biological functions of most proteins are more or less established, the one of methyltransferase WBSCR27 remains elusive. To find the substrate of methylation catalyzed by WBSCR27 we constructed mouse cell lines with a Wbscr27 gene knockout and studied the obtained cells using several molecular biology and mass spectrometry techniques. We attempted to pinpoint the methylation target among the RNAs and proteins, but in all cases neither a direct substrate has been identified nor the protein partners have been detected. To reveal the nature of the putative methylation substrate we determined the solution structure and studied the conformational dynamic properties of WBSCR27 in apo state and in complex with S-adenosyl-L-homocysteine (SAH). The protein core was found to form a canonical Rossman fold common for Class I methyltransferases. N-terminus of the protein and the β6–β7 loop were disordered in apo-form, but binding of SAH induced the transition of these fragments to a well-formed substrate binding site. Analyzing the structure of this binding site allows us to suggest potential substrates of WBSCR27 methylation to be probed in further research.



1. Mariasina S. S. и др. Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function // Frontiers in Molecular Biosciences. 2022. Т. 9.


DO - 10.3389/fmolb.2022.865743

UR -

TI - Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function

T2 - Frontiers in Molecular Biosciences

AU - Mariasina, Sofia S.

AU - Chang, Chi-Fon

AU - Navalayeu, Tsimafei L.

AU - Chugunova, Anastasia A.

AU - Efimov, Sergey V.

AU - Zgoda, Viktor G.

AU - Ivlev, Vasily A.

AU - Dontsova, Olga A.

AU - Sergiev, Petr V.

AU - Polshakov, Vladimir I.

PY - 2022

DA - 2022/06/15

PB - Frontiers Media SA

VL - 9

SN - 2296-889X

ER -

BibTex |


doi = {10.3389/fmolb.2022.865743},

url = {},

year = 2022,

month = {jun},

publisher = {Frontiers Media {SA}},

volume = {9},

author = {Sofia S. Mariasina and Chi-Fon Chang and Tsimafei L. Navalayeu and Anastasia A. Chugunova and Sergey V. Efimov and Viktor G. Zgoda and Vasily A. Ivlev and Olga A. Dontsova and Petr V. Sergiev and Vladimir I. Polshakov},

title = {Williams-Beuren Syndrome Related Methyltransferase {WBSCR}27: From Structure to Possible Function},

journal = {Frontiers in Molecular Biosciences}


Mariasina, Sofia S., et al. “Williams-Beuren Syndrome Related Methyltransferase WBSCR27: From Structure to Possible Function.” Frontiers in Molecular Biosciences, vol. 9, June 2022. Crossref,