ID | 66884 |
FullText URL | |
Author |
Taniguchi, Rikako
Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Moriya, Yuto
Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Dohmae, Naoshi
Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science
Suzuki, Takehiro
Biomolecular Characterization Unit, Technology Platform Division, RIKEN Center for Sustainable Resource Science
Nakahara, Kengo
Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Kubota, Sho
Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
Takasugi, Nobumasa
Department of Medicinal Pharmacology, Graduate School of Medicine, Dentistry and Pharmaceutical Sciences, Okayama University
|
Abstract | Upregulation of nitric oxide (NO) production contributes to the pathogenesis of numerous diseases via S-nitro- sylation, a post-translational modification of proteins. This process occurs due to the oxidative reaction between NO and a cysteine thiol group; however, the extent of this reaction remains unknown. S-Nitrosylation of PRMT1, a major asymmetric arginine methyltransferase of histones and numerous RNA metabolic proteins, was induced by NO donor treatment. We found that nitrosative stress leads to S-nitrosylation of cysteine 119, located near the active site, and attenuates the enzymatic activity of PRMT1. Interestingly, RNA sequencing analysis revealed similarities in the changes in expression elicited by NO and PRMT1 inhibitors or knockdown. A comprehensive search for PRMT1 substrates using the proximity-dependent biotin identification method highlighted many known and new substrates, including RNA-metabolizing enzymes. To validate this result, we selected the RNA helicase DDX3 and demonstrated that arginine methylation of DDX3 is induced by PRMT1 and attenuated by NO treatment. Our results suggest the existence of a novel regulatory system associated with transcription and RNA metabolism via protein S-nitrosylation.
|
Keywords | Nitric oxide
S-Nitrosylation
Protein arginine methyltransferase 1 (PRMT1)
RNA metabolism
Dead-box helicase 3X-linxed (DDX3)
|
Published Date | 2024-03
|
Publication Title |
Journal of Pharmacological Sciences
|
Volume | volume154
|
Issue | issue3
|
Publisher | Japanese Pharmacological Society
|
Start Page | 209
|
End Page | 217
|
ISSN | 1347-8613
|
NCID | AA11806667
|
Content Type |
Journal Article
|
language |
English
|
OAI-PMH Set |
岡山大学
|
Copyright Holders | © 2024 The Authors.
|
File Version | publisher
|
PubMed ID | |
DOI | |
Web of Science KeyUT | |
Related Url | isVersionOf https://doi.org/10.1016/j.jphs.2023.12.012
|
License | http://creativecommons.org/licenses/by-nc-nd/4.0/
|
Funder Name |
Ministry of Education, Culture, Sports, Science and Technology
Smoking Research Foundation
Japan Science and Technology Agency
|
助成番号 | 22K19380
JPMJSP2126
|