Nomenclature
EC number
2.1.1.170
Systematic name
S-adenosyl-l-methionine:16S rRNA (guanine527-N7)-methyltransferase
Recommended name
16S rRNA (guanine527-N7)-methyltransferase
Synonyms
16S rRNA methyltransferase <5> [2]
16S rRNA methyltransferase RsmG <4> [6]
gidB <2,4,6> (<2,4> gene name [4,6]) [4,5,6]
glucose-inhibited division protein B <6> [5]
ribosomal RNA small subunit methyltransferase G <4> [6]
rsmG <4,5> (<4,5> gene name [2,6]) [2,6]
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References
Tanaka, Y.; Tokuyama, S.; Ochi, K.: Activation of secondary metabolite-bio-synthetic gene clusters by generating rsmG mutations in Streptomyces griseus. J. Antibiot., 62, 669-673 (2009)
Nishimura, K.; Hosaka, T.; Tokuyama, S.; Okamoto, S.; Ochi, K.: Mutations in rsmG, encoding a 16S rRNA methyltransferase, result in low-level streptomycin resistance and antibiotic overproduction in Streptomyces coelicolor A3(2). J. Bacteriol., 189, 3876-3883 (2007)
Nishimura, K.; Johansen, S.K.; Inaoka, T.; Hosaka, T.; Tokuyama, S.; Tahara, Y.; Okamoto, S.; Kawamura, F.; Douthwaite, S.; Ochi, K.: Identification of the RsmG methyltransferase target as 16S rRNA nucleotide G527 and characterization of Bacillus subtilis rsmG mutants. J. Bacteriol., 189, 6068-6073 (2007)
Okamoto, S.; Tamaru, A.; Nakajima, C.; Nishimura, K.; Tanaka, Y.; Tokuyama, S.; Suzuki, Y.; Ochi, K.: Loss of a conserved 7-methylguanosine modification in 16S rRNA confers low-level streptomycin resistance in bacteria. Mol. Microbiol., 63, 1096-1106 (2007)
Romanowski, M.J.; Bonanno, J.B.; Burley, S.K.: Crystal structure of the Escherichia coli glucose-inhibited division protein B (GidB) reveals a methyltransferase fold. Proteins, 47, 563-567 (2002)
Gregory, S.T.; Demirci, H.; Belardinelli, R.; Monshupanee, T.; Gualerzi, C.; Dahlberg, A.E.; Jogl, G.: Structural and functional studies of the Thermus thermophilus 16S rRNA methyltransferase RsmG. RNA, 15, 1693-1704 (2009)
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Schomburg, D., Schomburg, I. (2013). 16S rRNA (guanine527-N7)-methyltransferase 2.1.1.170. In: Schomburg, D., Schomburg, I. (eds) Class 2–3.2 Transferases, Hydrolases. Springer Handbook of Enzymes. Springer, Berlin, Heidelberg. https://doi.org/10.1007/978-3-642-36240-8_8
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