Interaction between RsgA and the ribosome.
RsgA is a unique GTP hydrolytic protein that is widely found in bacteria and plants, and is activated by the small subunit of the ribosome. Disruption of the gene for RsgA from the genome affects the growth of cells, the subunit association of the ribosome in cells and maturation of 16S ribosomal RNA. Here, we investigated the interaction between EscherichiacoliRsgA and the ribosome. Several antibiotics bound to the decoding center of the small subunit inhibited the ribosome-dependent GTPase activity of RsgA, suggesting that RsgA binds to the decoding center. Chemical footprinting was also performed to further investigate the interaction.
Kimura
Takatsugu
T
Department of Biochemistry and Biotechnology, Faculty of Agriculture and Life Science, Hirosaki University.
Takagi
Kuniaki
K
Kyoko
Hanawa-Suetsugu
HS
Kalachnyuk
Liliya
L
Muto
Akira
A
Himeno
Hyouta
H
D000900:Anti-Bacterial Agents / Q000494:pharmacology; D029968:Escherichia coli Proteins / Q000378:metabolism*; D020558:GTP Phosphohydrolases / Q000378:metabolism*; D054680:Ribosome Subunits, Small, Bacterial / Q000187:drug effects / Q000378:metabolism*
D000900:Anti-Bacterial Agents; D029968:Escherichia coli Proteins; D020558:GTP Phosphohydrolases; C467318:RsgA protein, E coli