Jump to content

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

From Wikipedia, the free encyclopedia
18S rRNA (adenine1779-N6/adenine1780-N6)-dimethyltransferase
Identifiers
EC no.2.1.1.183
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Search
PMCarticles
PubMedarticles
NCBIproteins

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 (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.
[edit]