16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase
| 16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| EC no. | 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 | ||||||||
| |||||||||
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 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[edit]
- ^ Helser TL, Davies JE, Dahlberg JE (September 1971). "Change in methylation of 16S ribosomal RNA associated with mutation to kasugamycin resistance in Escherichia coli". Nature. 233 (35): 12–4. doi:10.1038/newbio233012a0. PMID 4329247.
- ^ Helser TL, Davies JE, Dahlberg JE (January 1972). "Mechanism of kasugamycin resistance in Escherichia coli". Nature. 235 (53): 6–9. doi:10.1038/newbio235006a0. PMID 4336392.
- ^ van Buul CP, van Knippenberg PH (1985). "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. doi:10.1016/0378-1119(85)90204-5. PMID 3905517.
- ^ Formenoy LJ, Cunningham PR, Nurse K, Pleij CW, 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 (12): 1123–8. doi:10.1016/0300-9084(94)90040-x. PMID 7538324.
- ^ O'Farrell HC, Scarsdale JN, Rife JP (May 2004). "Crystal structure of KsgA, a universally conserved rRNA adenine dimethyltransferase in Escherichia coli". Journal of Molecular Biology. 339 (2): 337–53. doi:10.1016/j.jmb.2004.02.068. PMID 15136037.
- ^ Poldermans B, Roza L, Van Knippenberg PH (September 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". The Journal of Biological Chemistry. 254 (18): 9094–100. PMID 383712.
- ^ Demirci H, Belardinelli R, Seri E, Gregory ST, Gualerzi C, Dahlberg AE, Jogl G (May 2009). "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. doi:10.1016/j.jmb.2009.02.066. PMC 2679894. PMID 19285505.
- ^ Tu C, Tropea JE, Austin BP, Court DL, Waugh DS, Ji X (March 2009). "Structural basis for binding of RNA and cofactor by a KsgA methyltransferase". Structure. 17 (3): 374–85. doi:10.1016/j.str.2009.01.010. PMC 2672589. PMID 19278652.
External links[edit]
- 16S+rRNA+(adenine1518-N6/adenine1519-N6)-dimethyltransferase at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
