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PMID: 7937131 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

M.phi 3TII: a new monospecific DNA (cytosine-C5) methyltransferase with pronounced amino acid sequence similarity to a family of adenine-N6-DNA-methyltransferases.

Nucleic acids research ·Vol. 22 ·No. 20 ·1994-10-11 ·Pages 4066-72

Noyer-Weidner M, Walter J, Terschüren PA, Chai S, Trautner TA

Abstract

The temperate B.subtilis phages phi 3T and rho 11s code, in addition to the multispecific DNA (cytosine-C5) methyltransferases (C5-MTases) M.phi 3TI and M.rho 11sI, which were previously characterized, for the identical monospecific C5-MTases M.phi 3TII and M.rho 11sII. These enzymes modify the C to TCGA sites, a novel target specificity among C5-MTases. The primary sequence of M.phi 3TII (326 amino acids) shows all conserved motifs typical of the building plan of C5-MTases. The degree of relatedness between M.phi 3TII and all other mono- or multispecific C5-MTases ranges from 30-40% amino acid identity. Particularly M.phi 3TII does not show pronounced similarity to M.phi 3TI indicating that both MTase genes were not generated from one another but were acquired independently by the phage. The amino terminal part of the M.phi 3TII (preceding the variable region 'V'), which predominantly constitutes the catalytic domain of the enzyme, exhibits pronounced sequence similarity to the amino termini of a family of A-N6-MTases, which--like M.Taql--recognize the general sequence TNNA. This suggests that recently described similarities in the general three dimensional organization of C5- and A-N6-MTases imply divergent evolution of these enzymes originating from a common molecular ancestor.

MeSH Terms
Amino Acid Sequence Bacillus Phages/enzymology,genetics Bacillus subtilis/virology Base Sequence Conserved Sequence DNA (Cytosine-5-)-Methyltransferases/chemistry,genetics,metabolism DNA, Viral/metabolism Genes, Viral/genetics Methylation Molecular Sequence Data RNA, Messenger/biosynthesis RNA, Viral/biosynthesis Restriction Mapping Sequence Alignment Sequence Analysis, DNA Sequence Homology, Amino Acid Site-Specific DNA-Methyltransferase (Adenine-Specific)/chemistry,genetics,metabolism Substrate Specificity Viral Proteins/chemistry,genetics,metabolism Viral Structural Proteins/genetics
Chemicals
DNA, Viral RNA, Messenger RNA, Viral Viral Proteins Viral Structural Proteins DNA modification methylase phi3TII, Bacteriophage phi-3T DNA (Cytosine-5-)-Methyltransferases Site-Specific DNA-Methyltransferase (Adenine-Specific)
Authors & Affiliations
5 authors, click to expand affiliations / ORCID
Noyer-Weidner M
Max-Planck-Institut für molekulare Genetik, Berlin, Germany.
Walter J
Terschüren P A
Chai S
Trautner T A
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/22.20.4066
Published
1994-10-11
Pages
4066-72
Language
English
Region
England
NLM ID
0411011
PMCID
PMC331891
Subset
IM
Databases
GENBANK
X80202
Corrections
RepublishedIn
PMID: 7816649
External Links
PubMed source DOI: 10.1093/nar/22.20.4066 PMC Full Text View journal details
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