Nucleic Acids Research, Vol 27, Issue 15 3138-3145, Copyright © 1999 by Oxford University Press
R Reid, PJ Greene and DV Santi
The Escherichia coli fmu gene product has recently been determined to be
the 16S rRNA m(5)C 967 methyltransferase. As such, Fmu represents the first
protein identified as an S -adenosyl-L-methionine (AdoMet)- dependent RNA
m(5)C methyltransferase whose amino acid sequence is known. Using the amino
acid sequence of Fmu as an initial probe in an iterative search of
completed DNA sequence databases, 27 homologous ORF products were
identified as probable RNA m(5)C methyltransferases. Further analysis of
sequences in undeposited genomic sequencing data and EST databases yielded
more than 30 additional homologs. These putative RNA m(5)C
methyltransferases are grouped into eight subfamilies, some of which are
predicted to consist of direct genetic counterparts, or orthologs. The
enzymes proposed to be RNA m(5)C methyltransferases have sequence motifs
closely related to signature sequences found in the well-studied DNA m(5)C
methyltransferases and other AdoMet-dependent methyltransferases.
Structure-function correlates in the known AdoMet methyltransferases
support the assignment of this family as RNA m(5)C methyltransferases.
ARTICLES
Exposition of a family of RNA m(5)C methyltransferases from searching genomic and proteomic sequences
Department of Pharmaceutical Chemistry, University of California, San Francisco, CA 94143-0448, USA.
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