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Literature summary for 2.8.4.4 extracted from

  • Strader, M.; Costantino, N.; Elkins, C.; Chen, C.; Patel, I.; Makusky, A.; Choy, J.; Court, D.; Markey, S.; Kowalak, J.
    A proteomic and transcriptomic approach reveals new insight into beta-methylthiolation of Escherichia coli ribosomal protein (2011), Mol. Cell. Proteomics, 10, M110.005199.
    View publication on PubMedView publication on EuropePMC

Organism

Organism UniProt Comment Textmining
Escherichia coli P0AEI4
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Escherichia coli W3110 / ATCC 27325 P0AEI4
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Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine substrate Escherichia coli S12 is modified at residue Asp88 Escherichia coli 3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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Asp88-[ribosomal protein S12] + sulfur-(sulfur carrier) + 2 S-adenosyl-L-methionine substrate Escherichia coli S12 is modified at residue Asp88 Escherichia coli W3110 / ATCC 27325 3-methylthioaspartate88-[ribosomal protein S12] + S-adenosyl-L-homocysteine + (sulfur carrier) + L-methionine + 5'-deoxyadenosine
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General Information

General Information Comment Organism
physiological function proteins RimO and YcaO, a conserved protein of unknown function, dramatically impact the modification status of ribosomal protein S12. The YcaO protein is involved in beta-methylthiolation of S12 and its absence impairs the ability of RimO to modify S12. The Escherichia coli specific beta-methylthiolation likely occurs when S12 is assembled as part of a ribosomal subunit. A RimO knockout mutant under aerobic conditions exhibits a 2fold decrease in transcription levels for a subset of genes belonging to operons that require the fumarate and nitrate reductase regulator for transcriptional activation and at least one of the nitrate and nitrite transcriptional response regulators NarL and NarP Escherichia coli