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PMID: 2204026 Published · ppublish English Journal Article

Cloning and nucleotide sequence of the genes coding for the Sau96I restriction and modification enzymes.

Nucleic acids research ·Vol. 18 ·No. 16 ·1990-08-25 ·Pages 4659-64

Szilák L, Venetianer P, Kiss A

Abstract

The genes coding for the GGNCC specific Sau96I restriction and modification enzymes were cloned and expressed in E. coli. The DNA sequence predicts a 430 amino acid protein (Mr: 49,252) for the methyltransferase and a 261 amino acid protein (Mr: 30,486) for the endonuclease. No protein sequence similarity was detected between the Sau96I methyltransferase and endonuclease. The methyltransferase contains the sequence elements characteristic for m5C-methyltransferases. In addition to this, M.Sau96I shows similarity, also in the variable region, with one m5C-methyltransferase (M.SinI) which has closely related recognition specificity (GGA/TCC). M.Sau96I methylates the internal cytosine within the GGNCC recognition sequence. The Sau96I endonuclease appears to act as a monomer.

MeSH Terms
Amino Acid Sequence Base Sequence Cloning, Molecular DNA Modification Methylases/genetics DNA, Bacterial/genetics,metabolism Deoxyribonucleases, Type II Site-Specific/genetics Escherichia coli/genetics Gene Expression Regulation, Bacterial Genes, Bacterial Methylation Molecular Sequence Data Restriction Mapping Sequence Homology, Nucleic Acid
Chemicals
DNA, Bacterial DNA Modification Methylases Deoxyribonucleases, Type II Site-Specific GGNCC-specific type II deoxyribonucleases
Authors & Affiliations
3 authors, click to expand affiliations / ORCID
Szilák L
Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Szeged.
Venetianer P
Kiss A
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Article Info
Journal
Nucleic acids research
Abbr.
Nucleic Acids Res
ISSN
0305-1048
DOI
10.1093/nar/18.16.4659
Published
1990-08-25
Pages
4659-64
Language
English
Region
England
NLM ID
0411011
PMCID
PMC331911
Subset
IM
Databases
GENBANK
X53096
External Links
PubMed source DOI: 10.1093/nar/18.16.4659 PMC Full Text View journal details
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