Sequential order of target‐recognizing domains in multispecific DNA‐methyltransferases

In the multispecific DNA(cytosine‐5)‐methyltransferases (Mtases) of Bacillus subtilis phages SPR and phi 3T the domains responsible for recognition of DNA methylation targets CCA/TGG, CCGG, GGCC (SPR) and GCNGC, GGCC (phi 3T) represent contiguous sequences of approximately 50 amino acids each. These...

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Bibliographic Details
Published in:The EMBO journal 1988-08, Vol.7 (8), p.2601-2609
Main Authors: Wilke, K., Rauhut, E., Noyer‐Weidner, M., Lauster, R., Pawlek, B., Behrens, B., Trautner, T. A.
Format: Article
Language:English
Subjects:
Amino Acid Sequence
Analytical, structural and metabolic biochemistry
Bacillus subtilis
Bacteriophages - enzymology
Bacteriophages - genetics
Base Sequence
Biological and medical sciences
Cross Reactions
DNA (Cytosine-5-)-Methyltransferases - genetics
DNA (Cytosine-5-)-Methyltransferases - metabolism
DNA, Viral - genetics
DNA, Viral - metabolism
Enzymes and enzyme inhibitors
Fundamental and applied biological sciences. Psychology
Methylation
Molecular Sequence Data
Mutation
Phenotype
Plasmids
Transferases
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Summary:In the multispecific DNA(cytosine‐5)‐methyltransferases (Mtases) of Bacillus subtilis phages SPR and phi 3T the domains responsible for recognition of DNA methylation targets CCA/TGG, CCGG, GGCC (SPR) and GCNGC, GGCC (phi 3T) represent contiguous sequences of approximately 50 amino acids each. These domains are tandemly arranged and do not overlap. They are part of a ‘variable’ segment within the enzymes which is flanked by ‘conserved’ amino acids, which are very similar amongst bacterial monospecific and the multispecific Mtases studied here. These results follow from a mutational analysis of the SPR and phi 3T Mtase genes. They further support our concept of a modular enzyme organization, according to which variability of type II Mtases with respect to target recognition is achieved by a combination of the same enzyme core with a variety of target‐recognizing domains.
ISSN:0261-4189
1460-2075
DOI:10.1002/j.1460-2075.1988.tb03110.x