FEBS Journal, volume 287, issue 24, pages 5375-5393

Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage

Publication typeJournal Article
Publication date2020-04-20
Journal: FEBS Journal
Quartile SCImago
Q1
Quartile WOS
Q2
Impact factor5.4
ISSN1742464X, 14321033
Biochemistry
Molecular Biology
Cell Biology
Abstract

Williams–Beuren syndrome, characterized by numerous physiological and mental problems, is caused by the heterozygous deletion of chromosome region 7q11.23, which results in the disappearance of 26 protein‐coding genes. Protein WBSCR27 is a product of one of these genes whose biological function has not yet been established and for which structural information has been absent until now. Using NMR, we investigated the structural and functional properties of murine WBSCR27. For protein in the apo form and in a complex with S‐(5′‐adenosyl)‐l‐homocysteine (SAH), a complete NMR resonance assignment has been obtained and the secondary structure has been determined. This information allows us to attribute WBSCR27 to Class I methyltransferases. The interaction of WBSCR27 with the cofactor S‐(5′‐adenosyl)‐l‐methionine (SAM) and its metabolic products – SAH, 5′‐deoxy‐5′‐methylthioadenosine (MTA) and 5′‐deoxyadenosine (5′dAdo) – was studied by NMR and isothermal titration calorimetry. SAH binds WBSCR27 much tighter than SAM, leaving open the question of cofactor turnover in the methylation reaction. One possible answer to this question is the presence of weak but detectable nucleosidase activity for WBSCR27. We found that the enzyme catalyses the cleavage of the adenine moiety from SAH, MTA and 5′dAdo, similar to the action of bacterial SAH/MTA nucleosidases. We also found that the binding of SAM or SAH causes a significant change in the structure of WBSCR27 and in the conformational mobility of the protein fragments, which can be attributed to the substrate recognition site. This indicates that the binding of the cofactor modulates the folding of the substrate‐recognizing region of the enzyme.

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Mariasina S. S. et al. Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage // FEBS Journal. 2020. Vol. 287. No. 24. pp. 5375-5393.
GOST all authors (up to 50) Copy
Mariasina S. S., Chang C., Petrova O. A., Efimov S., Klochkov V. V., Kechko O. I., Митькевич В. А., Sergiev P. V., Dontsova O. A., Polshakov V. I. Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage // FEBS Journal. 2020. Vol. 287. No. 24. pp. 5375-5393.
RIS |
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RIS Copy
TY - JOUR
DO - 10.1111/febs.15320
UR - https://doi.org/10.1111%2Ffebs.15320
TI - Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage
T2 - FEBS Journal
AU - Mariasina, Sofia S
AU - Chang, Chi-Fon
AU - Petrova, Olga A
AU - Kechko, Olga I.
AU - Dontsova, Olga A.
AU - Polshakov, Vladimir I.
AU - Efimov, Sergey
AU - Klochkov, V V
AU - Митькевич, В. А.
AU - Sergiev, Petr V.
PY - 2020
DA - 2020/04/20 00:00:00
PB - Wiley
SP - 5375-5393
IS - 24
VL - 287
SN - 1742-464X
SN - 1432-1033
ER -
BibTex |
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BibTex Copy
@article{2020_Mariasina
author = {Sofia S Mariasina and Chi-Fon Chang and Olga A Petrova and Olga I. Kechko and Olga A. Dontsova and Vladimir I. Polshakov and Sergey Efimov and V V Klochkov and В. А. Митькевич and Petr V. Sergiev},
title = {Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage},
journal = {FEBS Journal},
year = {2020},
volume = {287},
publisher = {Wiley},
month = {apr},
url = {https://doi.org/10.1111%2Ffebs.15320},
number = {24},
pages = {5375--5393},
doi = {10.1111/febs.15320}
}
MLA
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Mariasina, Sofia S., et al. “Williams–Beuren syndrome-related methyltransferase WBSCR27: cofactor binding and cleavage.” FEBS Journal, vol. 287, no. 24, Apr. 2020, pp. 5375-5393. https://doi.org/10.1111%2Ffebs.15320.
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