BCDIN3D Human

BCDIN3D contains an S-(5′-adenosyl)-L-methionine (AdoMet) binding motif, which is characteristic of eukaryotic protein methyltransferases . The enzyme recognizes unique structural features of cytoplasmic tRNA^His and discriminates it from other tRNA species . The methylation of the 5′-phosphate group of tRNA^His by BCDIN3D does not significantly affect its aminoacylation or stability, suggesting that this modification might be involved in unknown biological processes beyond protein synthesis .

BCDIN3D is overexpressed in breast cancer cells, and its high expression levels are associated with poor prognosis in triple-negative breast cancer . The enzyme’s role in cancer is linked to its ability to methylate specific precursor microRNAs (pre-miRNAs), such as tumor suppressor miR145 and miR23b . This methylation process is thought to contribute to the tumorigenic phenotype observed in breast cancer .

Recombinant human BCDIN3D is typically expressed in E. coli and purified using conventional chromatography techniques . The recombinant protein often includes an N-terminal His-tag to facilitate purification and detection . It is used in various research applications to study the enzyme’s function and its role in RNA methylation and cancer biology .

Recent studies have employed advanced sequencing methods to identify RNAs that stably bind to BCDIN3D, revealing interactions with full-length phospho-methylated tRNA^His and specific microRNAs . These findings provide insights into the enzyme’s substrate specificity and its potential regulatory roles in cellular processes .