gida

GidA, short for glucose-inhibited division A, is a highly conserved bacterial protein that participates in a critical post-transcriptional modification of transfer RNA (tRNA). The gidA gene encodes the GidA protein, which often operates in partnership with MnmE (also known as TrmE) to modify uridine 34 at the wobble position of a subset of tRNAs.

In the GidA–MnmE system, the two proteins cooperate to form the cmnm5s2U34 (or mnm5s2U34) modification on tRNA. This modification improves codon–anticodon pairing and helps ensure accurate and efficient decoding of specific codons, thereby supporting proper translation under a range of growth conditions. The process is part of a broader tRNA modification pathway that is responsive to cellular metabolism and stress.

GidA is typically described as a flavin-containing enzyme that functions in concert with the GTPase activity of MnmE. The exact biochemical steps are complex, but the overall outcome is the production of a modified wobble uridine essential for decoding certain NNA codons.

Genetically, gidA is known as glucose-inhibited division A due to early observations in Escherichia coli linking gidA function to cell division under high glucose conditions. Mutations in gidA can affect growth, tRNA modification, and, in some pathogenic bacteria, virulence and stress responses. GidA is widespread in bacteria and is often found in operons with mnmE, reflecting their related roles in tRNA modification.