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PMID: 2108858 Published · ppublish English Comparative Study Journal Article Research Support, Non-U.S. Gov't

The amino acid sequence of the CCGG recognizing DNA methyltransferase M.BsuFI: implications for the analysis of sequence recognition by cytosine DNA methyltransferases.

The EMBO journal ·Vol. 9 ·No. 4 ·1990-04-00 ·Pages 1007-13

Walter J, Noyer-Weidner M, Trautner TA

Abstract

The Bacillus subtilis FI DNA methyltransferase (M.BsuFI) modifies the outer cytosine of the DNA sequence CCGG, causing resistance against R.BsuFI and R.MspI restriction. The M.BsuFI gene was cloned and expressed in B.subtilis and Escherichia coli. As derived from the nucleotide sequence, the M.BsuFI protein has 409 amino acids, corresponding to a molecular mass of 46,918 daltons. Including these data we have compared the nucleotide and amino acid sequences of different CCGG recognizing enzymes. These analyses showed that M.BsuFI is highly related to two other CCGG specific methyltransferases, M.MspI and M.HpaII, which were isolated from Gram-negative bacteria. Between M.BsuFI and M.MspI the sequence similarity is particularly significant in a region, which has been postulated to contain the target recognition domains (TRDs) of cytosine-specific DNA methyltransferases. Apparently M.BsuFI and M.MspI, derived from phylogenetic distant organisms, use highly conserved structural elements for the recognition of the CCGG target sequence. In contrast the very same region of M.HpaII is quite different from those of M.BsuFI and M.MspI. We attribute this difference to the different targeting of methylation within the sequence CCGG, where M.HpaII methylates the inner, M.BsuFI/M.MspI the outer cytosine. Also the CCGG recognizing TRD of the multispecific B.subtilis phage SPR Mtase is distinct from that of the host enzyme, possibly indicating different requirements for TRDs operative in mono- and multispecific enzymes.

MeSH Terms
Amino Acid Sequence Bacillus subtilis/enzymology,genetics Base Sequence Cloning, Molecular DNA (Cytosine-5-)-Methyltransferases/genetics,metabolism DNA-Cytosine Methylases/genetics,metabolism Genes, Bacterial Methylation Molecular Sequence Data Restriction Mapping Sequence Homology, Nucleic Acid Substrate Specificity
Chemicals
DNA modification methylase HpaII DNA-Cytosine Methylases DNA (Cytosine-5-)-Methyltransferases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Walter J
Max-Planck-Institut für molekulare Genetik, Berlin, FRG.
Noyer-Weidner M
Trautner T A
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44 references, click to expand
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Article Info
Journal
The EMBO journal
Abbr.
EMBO J
ISSN
0261-4189
Published
1990-04-00
Pages
1007-13
Language
English
Region
England
NLM ID
8208664
PMCID
PMC551770
Subset
IM
Databases
GENBANK
X51515
External Links
PubMed source PMC Full Text View journal details
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