Identification of substrates and sequence requirements for CARNMT1-mediated histidine methylation of C3H zinc fingers.

ABSTRACT: It has recently become clear that protein histidine methylation is widespread and functionally important in many cellular processes, and human CARNMT1 was recently reported as a novel protein histidine methyltransferase (HMT). We describe our independent uncovering of CARNMT1's protein HMT activity and a comprehensive assessment of its methylation targets and substrate specificity. Using a combination of in vitro methylation of cellular extracts and protein mass spectrometry, we identified several CARNMT1 substrates that were fully methylated in cells, all of which were C3H zinc finger (ZnF) proteins. These include the previously identified U2AF1, ZC3H15, and ZC3H18 but also the unreported RBM22, PPP1R10, PRR3, and RNF113A. Using peptide arrays, we investigated CARNMT1-mediated methylation

SUBMITTER: Malecki JM 

PROVIDER: S-EPMC12275196 | biostudies-literature | 2025 Jun

REPOSITORIES: biostudies-literature