{"title":"Commentary on: γ-enolase (ENO2) is methylated at the Nτ position of His-190 among enolase isozymes.","authors":"Mitsuharu Hattori","doi":"10.1093/jb/mvae088","DOIUrl":null,"url":null,"abstract":"<p><p>Post-translational modifications play crucial roles in regulating protein function. Protein methylation, occurring at lysine, arginine, and histidine, has gained attention, particularly for histone methylation. However, the mechanism and significance of protein methylation at histidine remains poorly understood. Kasai et al. developed a novel method to identify histidine-methylated proteins and discovered that γ-enolase in the mouse brain undergoes Nτ-methylation at His190. This modification reduces dimerization and enzymatic activity, suggesting this reaction plays a physiological role. This work will accelerate research on histidine methylation and help elucidate unknown phenomena in the brain.</p>","PeriodicalId":15234,"journal":{"name":"Journal of biochemistry","volume":" ","pages":""},"PeriodicalIF":2.1000,"publicationDate":"2024-12-16","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of biochemistry","FirstCategoryId":"99","ListUrlMain":"https://doi.org/10.1093/jb/mvae088","RegionNum":4,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q4","JCRName":"BIOCHEMISTRY & MOLECULAR BIOLOGY","Score":null,"Total":0}
引用次数: 0
Abstract
Post-translational modifications play crucial roles in regulating protein function. Protein methylation, occurring at lysine, arginine, and histidine, has gained attention, particularly for histone methylation. However, the mechanism and significance of protein methylation at histidine remains poorly understood. Kasai et al. developed a novel method to identify histidine-methylated proteins and discovered that γ-enolase in the mouse brain undergoes Nτ-methylation at His190. This modification reduces dimerization and enzymatic activity, suggesting this reaction plays a physiological role. This work will accelerate research on histidine methylation and help elucidate unknown phenomena in the brain.
期刊介绍:
The Journal of Biochemistry founded in 1922 publishes the results of original research in the fields of Biochemistry, Molecular Biology, Cell, and Biotechnology written in English in the form of Regular Papers or Rapid Communications. A Rapid Communication is not a preliminary note, but it is, though brief, a complete and final publication. The materials described in Rapid Communications should not be included in a later paper. The Journal also publishes short reviews (JB Review) and papers solicited by the Editorial Board.