16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase

16S rRNA (adenine^1518-N^6/adenine^1519-N^6)-dimethyltransferase
Identifiers
EC number	2.1.1.182
Databases
IntEnz	IntEnz view
BRENDA	BRENDA entry
ExPASy	NiceZyme view
KEGG	KEGG entry
MetaCyc	metabolic pathway
PRIAM	profile
PDB structures	RCSB PDB PDBe PDBsum
Search PMC articles PubMed articles NCBI proteins

16S rRNA (adenine¹⁵¹⁸-N⁶/adenine¹⁵¹⁹-N⁶)-dimethyltransferase (EC 2.1.1.182, S-adenosylmethionine-6-N',N'-adenosyl (rRNA) dimethyltransferase, KsgA, ksgA methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine¹⁵¹⁸-N⁶/adenine¹⁵¹⁹-N⁶)-dimethyltransferase.^{[1][2][3][4][5][6][7][8]} This enzyme catalyses the following chemical reaction

4 S-adenosyl-L-methionine + adenine¹⁵¹⁸/adenine¹⁵¹⁹ in 16S rRNA $\rightleftharpoons$ 4 Ribosomal RNA + N⁶-dimethyladenine¹⁵¹⁸/N⁶-dimethyladenine¹⁵¹⁹ in 16S rRNA

KsgA introduces the dimethylation of adenine¹⁵¹⁸ and adenine¹⁵¹⁹ in 16S rRNA. Strains lacking the methylase are resistant to kasugamycin [1].

References

1. Helser, T.L., Davies, J.E. and Dahlberg, J.E. (1971). "Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli". Nature New Biology 233: 12–14. doi:10.1038/newbio233012a0. PMID 4329247.
2. Helser, T.L., Davies, J.E. and Dahlberg, J.E. (1972). "Mechanism of kasugamycin resistance in Escherichia coli". Nature New Biology 235: 6–9. doi:10.1038/newbio235006a0. PMID 4336392.
3. van Buul, C.P. and van Knippenberg, P.H. (1985). "Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA". Gene 38: 65–72. doi:10.1016/0378-1119(85)90204-5. PMID 3905517.
4. Formenoy, L.J., Cunningham, P.R., Nurse, K., Pleij, C.W. and Ofengand, J. (1994). "Methylation of the conserved A¹⁵¹⁸-A¹⁵¹⁹ in Escherichia coli 16S ribosomal RNA by the ksgA methyltransferase is influenced by methylations around the similarly conserved U¹⁵¹².G¹⁵²³ base pair in the 3′ terminal hairpin". Biochimie 76: 1123–1128. doi:10.1016/0300-9084(94)90040-x. PMID 7538324.
5. O'Farrell, H.C., Scarsdale, J.N. and Rife, J.P. (2004). "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli". J. Mol. Biol. 339: 337–353. doi:10.1016/j.jmb.2004.02.068. PMID 15136037.
6. Poldermans, B., Roza, L. and Van Knippenberg, P.H. (1979). "Studies on the function of two adjacent N⁶,N⁶-dimethyladenosines near the 3′ end of 16 S ribosomal RNA of Escherichia coli. III. Purification and properties of the methylating enzyme and methylase-30 S interactions". J. Biol. Chem. 254: 9094–9100. PMID 383712.
7. Demirci, H., Belardinelli, R., Seri, E., Gregory, S.T., Gualerzi, C., Dahlberg, A.E. and Jogl, G. (2009). "Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5′-methylthioadenosine". J. Mol. Biol. 388: 271–282. doi:10.1016/j.jmb.2009.02.066. PMID 19285505.
8. Tu, C., Tropea, J.E., Austin, B.P., Court, D.L., Waugh, D.S. and Ji, X. (2009). "Structural basis for binding of RNA and cofactor by a KsgA methyltransferase". Structure 17: 374–385. doi:10.1016/j.str.2009.01.010. PMID 19278652.

External links

• 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase at the US National Library of Medicine Medical Subject Headings (MeSH)