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

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16S rRNA (adenine1518-N6/adenine1519-N6)-dimethyltransferase
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EC no. 2.1.1.182
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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 + adenine 1518/adenine 1519 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].

Related Research Articles

<span class="mw-page-title-main">Methyltransferase</span> Group of methylating enzymes

Methyltransferases are a large group of enzymes that all methylate their substrates but can be split into several subclasses based on their structural features. The most common class of methyltransferases is class I, all of which contain a Rossmann fold for binding S-Adenosyl methionine (SAM). Class II methyltransferases contain a SET domain, which are exemplified by SET domain histone methyltransferases, and class III methyltransferases, which are membrane associated. Methyltransferases can also be grouped as different types utilizing different substrates in methyl transfer reactions. These types include protein methyltransferases, DNA/RNA methyltransferases, natural product methyltransferases, and non-SAM dependent methyltransferases. SAM is the classical methyl donor for methyltransferases, however, examples of other methyl donors are seen in nature. The general mechanism for methyl transfer is a SN2-like nucleophilic attack where the methionine sulfur serves as the leaving group and the methyl group attached to it acts as the electrophile that transfers the methyl group to the enzyme substrate. SAM is converted to S-Adenosyl homocysteine (SAH) during this process. The breaking of the SAM-methyl bond and the formation of the substrate-methyl bond happen nearly simultaneously. These enzymatic reactions are found in many pathways and are implicated in genetic diseases, cancer, and metabolic diseases. Another type of methyl transfer is the radical S-Adenosyl methionine (SAM) which is the methylation of unactivated carbon atoms in primary metabolites, proteins, lipids, and RNA.

In enzymology, a rRNA (adenine-N6-)-methyltransferase (EC 2.1.1.48) is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (guanine-N1-)-methyltransferase (EC 2.1.1.51) is an enzyme that catalyzes the chemical reaction

In enzymology, a rRNA (guanine-N2-)-methyltransferase (EC 2.1.1.52) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (guanine-N7-)-methyltransferase (EC 2.1.1.33) is an enzyme that catalyzes the chemical reaction

In enzymology, a tRNA (uracil-5-)-methyltransferase is an enzyme that catalyzes the chemical reaction

23S rRNA (uridine2552-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (uridine2552-2'-O-)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine1835-N2)-methyltransferase (EC 2.1.1.174, ygjO (gene), rlmG (gene), ribosomal RNA large subunit methyltransferase G) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine1835-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine1407-C5)-methyltransferase (EC 2.1.1.178, RNA m5C methyltransferase YebU, RsmF, YebU) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1407-C5)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1405-N7)-methyltransferase (EC 2.1.1.179, methyltransferase Sgm, m7G1405 Mtase, Sgm Mtase, Sgm, sisomicin-gentamicin methyltransferase, sisomicin-gentamicin methylase, GrmA, RmtB, RmtC, ArmA) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1405-N7)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (adenine1408-N1)-methyltransferase (EC 2.1.1.180, kanamycin-apramycin resistance methylase, 16S rRNA:m1A1408 methyltransferase, KamB, NpmA, 16S rRNA m1A1408 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (adenine1408-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine1618-N6)-methyltransferase (EC 2.1.1.181, rRNA large subunit methyltransferase F, YbiN protein, rlmF (gene), m6A1618 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine1618-N6)-methyltransferase. This enzyme catalyses the following chemical reaction

18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase (EC 2.1.1.183, 18S rRNA dimethylase Dim1p, Dim1p, ScDim1, m2(6)A dimethylase, KIDIM1) is an enzyme with systematic name S-adenosyl-L-methionine:18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenine2085-N6)-dimethyltransferase (EC 2.1.1.184, ErmC' methyltransferase, ermC methylase, ermC 23S rRNA methyltransferase, rRNA:m6A methyltransferase ErmC', ErmC', rRNA methyltransferase ErmC' ) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenine2085-N6)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (guanine745-N1)-methyltransferase (EC 2.1.1.187, Rlma(I), Rlma1, 23S rRNA m1G745 methyltransferase, YebH, RlmAI methyltransferase, ribosomal RNA(m1G)-methylase, rRNA(m1G)methylase, RrmA, 23S rRNA:m1G745 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (guanine745-N1)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytidine1402-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytidine1402-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (cytosine1402-N4)-methyltransferase (EC 2.1.1.199, RsmH, MraW) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (cytosine1402-N4)-methyltransferase. This enzyme catalyses the following chemical reaction

TRNA (guanine26-N2)-dimethyltransferase (EC 2.1.1.216, Trm1p, TRM1, tRNA (m22G26)dimethyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:tRNA (guanine26-N2)-dimethyltransferase. This enzyme catalyses the following chemical reaction

23S rRNA (adenosine1067-2'-O)-methyltransferase is an enzyme with systematic name S-adenosyl-L-methionine:23S rRNA (adenosine1067-2'-O)-methyltransferase. This enzyme catalyses the following chemical reaction

16S rRNA (guanine1516-N2)-methyltransferase (EC 2.1.1.242, yhiQ (gene), rsmJ (gene), m2G1516 methyltransferase) is an enzyme with systematic name S-adenosyl-L-methionine:16S rRNA (guanine1516-N2)-methyltransferase. This enzyme catalyses the following chemical reaction

References

  1. 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.
  2. 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.
  3. 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.
  4. 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.
  5. 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.
  6. 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.
  7. 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.
  8. 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.