Comparison of Protein Structures Reveals Monophyletic Origin of the AdoMet-Dependent Methyltransferase Family and Mechanistic Convergence Rather than Recent Differentiation of N4-Cytosine and…

By Janusz M. Bujnicki. 2000

71 citations recorded by the source corpus.

Phylogenetic analysis of the S-adenosyl-L-methionine-dependent methyltransferases was performed based on similarity of positions of main chain á-carbon atoms in published structures of members of this superfamily. The evolutionary tree was inferred and the problem of mono/polyphyletic origin of DNA methyltransferases from the Rossmann-fold enzymes was solved, bridging two seemingly antithetical hypotheses. The comparison of protein structures provides evidence for an evolutionary link between widely diverged subfamilies of RNA and DNA N6-adenine methyltransferases and argues against the close homology of N6-adenine and N4-cytosine methyltransferases, apparent from biochemical data and comparison of fragments of sequences. Such evolutionary analysis of methyltransferases has never been published yet in the literature and will guide further phylogenetical studies based on both sequence and structure comparison.

Subfields: Molecular Biology

How researchers see this paper

The researchers whose trusted networks rank it highest, strongest advocate first. Every researcher gets a different order.

In Molecular Biology

Citations in the corpus

ECOD: An Evolutionary Classification of Protein Domains (2014, background): “Although both SCOP and CATH indicate by their classification that SAM MTases and Rossmann domains are not homologous, literature suggests that they are actually related [46,47].”