18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase

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18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
Identifiers
EC number 2.1.1.183
Databases
IntEnz IntEnz view
BRENDA BRENDA entry
ExPASy NiceZyme view
KEGG KEGG entry
MetaCyc metabolic pathway
PRIAM profile
PDB structures RCSB PDB PDBe PDBsum

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.[1][2][3][4][5] This enzyme catalyses the following chemical reaction

4 S-adenosyl-L-methionine + adenine1779/adenine1780 in 18S rRNA 4 S-adenosyl-L-homocysteine + N6-dimethyladenine1779/N6-dimethyladenine1780 in 18S rRNA

DIM1 is involved in pre-rRNA processing.

References[edit]

  1. ^ Lafontaine, D.; Vandenhaute, J.; Tollervey, D. (1995). "The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast". Genes Dev. 9: 2470–2481. doi:10.1101/gad.9.20.2470. PMID 7590228. 
  2. ^ Lafontaine, D.L.; Preiss, T.; Tollervey, D. (1998). "Yeast 18S rRNA dimethylase Dim1p: a quality control mechanism in ribosome synthesis". Mol. Cell. Biol. 18: 2360–2370. doi:10.1128/mcb.18.4.2360. PMC 121492Freely accessible. PMID 9528805. 
  3. ^ Pulicherla, N.; Pogorzala, L.A.; Xu, Z.; O'Farrell, H.C.; Musayev, F.N.; Scarsdale, J.N.; Sia, E.A.; Culver, G.M.; Rife, J.P. (2009). "Structural and functional divergence within the Dim1/KsgA family of rRNA methyltransferases". J. Mol. Biol. 391: 884–893. doi:10.1016/j.jmb.2009.06.015. PMC 2753216Freely accessible. PMID 19520088. 
  4. ^ Lafontaine, D.; Delcour, J.; Glasser, A.L.; Desgres, J.; Vandenhaute, J. (1994). "The DIM1 gene responsible for the conserved m6(2)Am6(2)A dimethylation in the 3′-terminal loop of 18 S rRNA is essential in yeast". J. Mol. Biol. 241: 492–497. doi:10.1006/jmbi.1994.1525. PMID 8064863. 
  5. ^ O'Farrell, H.C.; Pulicherla, N.; Desai, P.M.; Rife, J.P. (2006). "Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution". RNA. 12: 725–733. doi:10.1261/rna.2310406. PMC 1440906Freely accessible. PMID 16540698. 

External links[edit]