5'-terminal glycosylation of protein-coding transcripts: An epitranscriptomic modification that prolongs mRNA lifetimes.

ABSTRACT: Glycosylation is among the most common molecular modifications in living organisms, one that affects the function of myriad macromolecules: mostly proteins, lipids, and polysaccharides of various kinds but also a few specific noncoding RNAs that undergo glycosylation at an internal site. Here we expand the glycome by showing that protein-coding transcripts can also be glycosylated, but in the form of a 5'-terminal glucose cap. These caps are present on up to 30 to 40% of the 5' ends of U-initiated mRNAs in Escherichia coli, a remarkably high level of noncanonical capping that requires no transcript or promoter characteristic other than a 5'-terminal U. By contrast, no N-acetylglucosamine caps are evident. Due to their resistance to enzymatic removal, glucose caps can greatly

SUBMITTER: Banerjee T 

PROVIDER: S-EPMC12541447 | biostudies-literature | 2025 Oct

REPOSITORIES: biostudies-literature