Dysregulation of a nucleotidyltransferase induces division and surface glycan defects in <i>Escherichia coli</i> by altering related metabolite levels.

ABSTRACT: The cell surface of gram-negative Escherichia coli is rich in glycoconjugates, including O-antigen (O-Ag) and enterobacterial common antigen polysaccharides, which mediate interactions with the environment. Enzymes called nucleotidyltransferases produce nucleoside diphosphate sugars (NDP-sugars), the precursors to these and many other cellular glycans. Across bacteria, glucose-1-phosphate thymidylyltransferases (G1P-Ts) couple deoxythymidine triphosphate (dTTP) and glucose-1-phosphate to produce a key secondary metabolite, deoxythymidine diphosphate-glucose (dTDP-Glc). Flux through many glycan biosynthetic pathways is regulated through feedback inhibition at an allosteric site of the conserved bacterial G1P-T RmlA. Here, we sought to address the cellular consequences of G1P-T dysreg

SUBMITTER: Zheng MC 

PROVIDER: S-EPMC12773781 | biostudies-literature | 2026 Jan

REPOSITORIES: biostudies-literature