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

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

  1. ↑ Lafontaine D, Vandenhaute J, Tollervey D (October 1995). "The 18S rRNA dimethylase Dim1p is required for pre-ribosomal RNA processing in yeast". Genes & Development. 9 (20): 2470–81. doi:10.1101/gad.9.20.2470. PMID 7590228.
  2. ↑ Lafontaine DL, Preiss T, Tollervey D (April 1998). "Yeast 18S rRNA dimethylase Dim1p: a quality control mechanism in ribosome synthesis?". Molecular and Cellular Biology. 18 (4): 2360–70. doi:10.1128/mcb.18.4.2360. PMC 121492. PMID 9528805.
  3. ↑ Pulicherla N, Pogorzala LA, Xu Z, O Farrell HC, Musayev FN, Scarsdale JN, Sia EA, Culver GM, Rife JP (September 2009). "Structural and functional divergence within the Dim1/KsgA family of rRNA methyltransferases". Journal of Molecular Biology. 391 (5): 884–93. doi:10.1016/j.jmb.2009.06.015. PMC 2753216. PMID 19520088.
  4. ↑ Lafontaine D, Delcour J, Glasser AL, Desgrès J, Vandenhaute J (August 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". Journal of Molecular Biology. 241 (3): 492–7. doi:10.1006/jmbi.1994.1525. PMID 8064863.
  5. ↑ O'Farrell HC, Pulicherla N, Desai PM, Rife JP (May 2006). "Recognition of a complex substrate by the KsgA/Dim1 family of enzymes has been conserved throughout evolution". Rna. 12 (5): 725–33. doi:10.1261/rna.2310406. PMC 1440906. PMID 16540698.
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