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Structural and Dynamic Insights into Redundant Function of YTHDF Proteins


Li, Yaozong; Bedi, Rajiv K; Moroz-Omori, Elena V; Caflisch, Amedeo (2020). Structural and Dynamic Insights into Redundant Function of YTHDF Proteins. Journal of Chemical Information and Modeling, 60(12):5932-5935.

Abstract

Three YTH-domain family proteins (YTHDF1, YTHDF2, and YTHDF3) recognize the N$^{6}$-methyladenosine (m$^{6}$A) modification of mRNA in cells. However, the redundancy of their cellular functions has been disputed. We investigate their interactions with m$^{6}$A-containing RNA using X-ray crystallography and molecular dynamics (MD). The new X-ray structures and MD simulations show that the three proteins share identical interactions with the m$^{6}$A-containing RNA and have similar intrinsic plasticity, thus evidencing the redundant roles of the three proteins in cellular functions.

Abstract

Three YTH-domain family proteins (YTHDF1, YTHDF2, and YTHDF3) recognize the N$^{6}$-methyladenosine (m$^{6}$A) modification of mRNA in cells. However, the redundancy of their cellular functions has been disputed. We investigate their interactions with m$^{6}$A-containing RNA using X-ray crystallography and molecular dynamics (MD). The new X-ray structures and MD simulations show that the three proteins share identical interactions with the m$^{6}$A-containing RNA and have similar intrinsic plasticity, thus evidencing the redundant roles of the three proteins in cellular functions.

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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > Department of Biochemistry
07 Faculty of Science > Department of Biochemistry
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Scopus Subject Areas:Physical Sciences > General Chemistry
Physical Sciences > General Chemical Engineering
Physical Sciences > Computer Science Applications
Social Sciences & Humanities > Library and Information Sciences
Language:English
Date:28 December 2020
Deposited On:27 Jan 2021 15:41
Last Modified:28 Jan 2021 21:02
Publisher:American Chemical Society (ACS)
ISSN:1549-9596
OA Status:Closed
Publisher DOI:https://doi.org/10.1021/acs.jcim.0c01029
PubMed ID:33073985

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