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Structural characterization of two tandemly arranged DNA methyltransferase genes from Neisseria gonorrhoeae MS11: N4‐cytosine specific M. Ngo MXV and nonfunctional 5‐cytosine‐type M. Ngo Morf2P
Author(s) -
Radlinska Monika,
Bujnicki Janusz M.,
Piekarowicz Andrzej
Publication year - 1999
Publication title -
proteins: structure, function, and bioinformatics
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.699
H-Index - 191
eISSN - 1097-0134
pISSN - 0887-3585
DOI - 10.1002/(sici)1097-0134(19991201)37:4<717::aid-prot20>3.0.co;2-p
Subject(s) - cytosine , gene , genetics , biology , dna , dna methyltransferase , dna sequencing , sequence alignment , methyltransferase , peptide sequence , methylation
Two adjacent genes encoding DNA methyltransferases (MTases) of Neisseria gonorrhoeae MS11, an active N4‐cytosine specific M. Ngo MXV and an inactive 5‐cytosine type M. Ngo Morf2P, were cloned into Escherichia coli and sequenced. We analyzed the deduced amino acid sequence of both gene products and localized conserved regions characteristic for DNA MTases. Structure prediction, threading‐derived alignments, and comparison with the common fold for DNA MTases allowed for construction of super‐secondary and tertiary models for M. Ngo Morf2P and M. Ngo MXV, respectively. These models helped in identification of amino acids and structural elements essential for function of both enzymes. The implications of this putative structural model on the catalytic mechanism of M. Ngo MXV and its possible relation to the common ancestor of modern DNA amino‐MTases are also discussed. Proteins 1999;37:717–728. ©1999 Wiley‐Liss, Inc.