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Phylogenomic analysis of 16S rRNA:(guanine‐N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino‐methyltransferases
Author(s) -
BUJNICKI JANUSZ M.
Publication year - 2000
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fj.00-0076com
Subject(s) - methyltransferase , biology , conserved sequence , genetics , sequence logo , phylogenetic tree , subfamily , methylation , rna , ribosomal rna , sequence alignment , 16s ribosomal rna , dna , peptide sequence , gene , base sequence
The sequences of known Escherichia coli 16S rRNA:m 2 G1207 methyltransferase (MTase) RsmC and hypothetical 16S rRNA:m 2 G966 MTase encoded by the ygjo open reading frame were used to carry out a database search of other putative m 2 G‐generating enzymes in finished and unfinished genomic sequences. Sequence comparison and phy‐logenetic analysis of 21 close homologs of RsmC and YgjO revealed the presence of the third paralogous lineage in E. coli and other γ‐Proteobacteria, which might correspond to the subfamily of MTases spe¬cific for G1516 in 16S rRNA. In addition, the com¬parative sequence analysis supported by sequence/ structure threading suggests that rRNA:m 2 G MTases are very closely related to RNA and DNA:m 6 A MTases and that these two enzyme families share common architecture of the active site and presum‐ably a similar mechanism of methyl group transfer onto the exocyclic amino group of their target bases.—Bujnicki, J. M. Phylogenomic analysis of 16S rRNA:(guanine‐N2) methyltransferases suggests new family members and reveals highly conserved motifs and a domain structure similar to other nucleic acid amino‐methyltransferases. FASEB J. 14, 2365‐2368 (2000)