PS01131

Ribosomal RNA adenine dimethylases signature

PROSITE patterns entry
Member databasePROSITE patterns
PROSITE patterns typeconserved site
Short nameRRNA_A_DIMETH

Description

A number of enzymes responsible for the dimethylation of adenosines in ribosomal RNAs (EC 2.1.1.48) have been found
[1]
to be evolutionary related. These enzymes are: - Bacterial 16S rRNA dimethylase (gene ksgA), which acts in the biogenesis of ribosomes by catalyzing the dimethylation of two adjacent adenosines in the loop of a conserved hairpin near the 3'-end of 16S rRNA. Inactivation of ksgA leads to resistance to the aminoglycoside antibiotic kasugamycin. - Yeast 18S rRNA dimethylase (gene DIM1), which is functionally similar to ksgA and that dimethylates twin adenosines in the 3'-end of 18S rRNA. - Bacterial 'erm' methylases. These enzymes confer resistance to macrolide- lincosamide-streptogramin B (MLS) antibiotics - such as erythromycin - by dimethylating the adenine residue at position 2058 of 23S rRNA thus resulting in a reduced affinity between ribosomes and the MLS antibiotics. - Caenorhabditis elegans hypothetical protein EO2H1.1. The best conserved region in these enzymes is located in the N-terminal section and corresponds to a region that is probably involved in S-adenosyl methionine (SAM) binding.

References

1.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. Lafontaine D, Delcour J, Glasser AL, Desgres J, Vandenhaute J. J. Mol. Biol. 241, 492-7, (1994). View articlePMID: 8064863

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