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

Class of enzymes 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase 2.1.1.182 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase (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. Helser TL, Davies JE, Dahlberg JE Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli Nature 233 35 12–4 September 1971 4329247 10.1038/newbio233012a0 Helser TL, Davies JE, Dahlberg JE Mechanism of kasugamycin resistance in Escherichia coli Nature 235 53 6–9 January 1972 4336392 10.1038/newbio235006a0 van Buul CP, van Knippenberg PH Nucleotide sequence of the ksgA gene of Escherichia coli: comparison of methyltransferases effecting dimethylation of adenosine in ribosomal RNA Gene 38 1–3 65–72 1985 3905517 10.1016/0378-1119(85)90204-5 Formenoy LJ, Cunningham PR, Nurse K, Pleij CW, Ofengand J 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 12 1123–8 1994 7538324 10.1016/0300-9084(94)90040-x O'Farrell HC, Scarsdale JN, Rife JP Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli Journal of Molecular Biology 339 2 337–53 May 2004 15136037 10.1016/j.jmb.2004.02.068 Poldermans B, Roza L, Van Knippenberg PH 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 The Journal of Biological Chemistry 254 18 9094–100 September 1979 10.1016/S0021-9258(19)86815-1 free 383712 Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G Structural rearrangements in the active site of the Thermus thermophilus 16S rRNA methyltransferase KsgA in a binary complex with 5'-methylthioadenosine Journal of Molecular Biology 388 2 271–82 May 2009 19285505 2679894 10.1016/j.jmb.2009.02.066 Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X Structural basis for binding of RNA and cofactor by a KsgA methyltransferase Structure 17 3 374–85 March 2009 19278652 2672589 10.1016/j.str.2009.01.010 This enzyme catalyses the following chemical reaction 4 S-adenosyl-L-methionine + adenine1518/adenine1519 in 16S rRNA 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 External links 16S+rRNA+(adenine1518-N6/adenine1519-N6)-dimethyltransferase Biology no Category:EC 2.1.1