Biomaterial Database

Cloning and characterization of Sse9I DNA-methyltransferase recognizing 5'-AATT-3'. 1996

D A Gonchar, and Y I Wolf, and S Kh Degtyarev

SibEnzyme, Novosibirsk, Russia.

The gene from Sporosarcina species 9D encoding Sse9I DNA-methyltransferase (M.Sse9I) was cloned and expressed in Escherichia coli. The recombinant plasmid pMSse-1 contains the M.Sse9I gene 1086 bp in length, corresponding to a protein of 362 amino acid residues. M.Sse9I recognizes the tetranucleotide sequence 5'-AATT-3' and modifies the second adenine within the recognition sequence. The amino acid sequence of M.Sse9I was compared with those of other methylases. According to mutual positions of four conservative domains the new enzyme belongs to a subgroup of D12 class. This subgroup includes Sse9I, CviAII, NlaIII and N-terminal domains of LlaI, FokI and StsI DNA-methyltransferases.

UI	MeSH Term	Description	Entries
D008969	Molecular Sequence Data	Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.	Sequence Data, Molecular,Molecular Sequencing Data,Data, Molecular Sequence,Data, Molecular Sequencing,Sequencing Data, Molecular
D003001	Cloning, Molecular	The insertion of recombinant DNA molecules from prokaryotic and/or eukaryotic sources into a replicating vehicle, such as a plasmid or virus vector, and the introduction of the resultant hybrid molecules into recipient cells without altering the viability of those cells.	Molecular Cloning
D004269	DNA, Bacterial	Deoxyribonucleic acid that makes up the genetic material of bacteria.	Bacterial DNA
D006095	Gram-Positive Cocci	Coccus-shaped bacteria that retain the crystal violet stain when treated by Gram's method.	Gram Positive Cocci
D000225	Adenine	A purine base and a fundamental unit of ADENINE NUCLEOTIDES.	Vitamin B 4,4, Vitamin B,B 4, Vitamin
D000595	Amino Acid Sequence	The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.	Protein Structure, Primary,Amino Acid Sequences,Sequence, Amino Acid,Sequences, Amino Acid,Primary Protein Structure,Primary Protein Structures,Protein Structures, Primary,Structure, Primary Protein,Structures, Primary Protein
D001420	Bacteria, Aerobic	Bacteria which require oxygen in order to grow and survive.	Aerobic Bacteria
D001483	Base Sequence	The sequence of PURINES and PYRIMIDINES in nucleic acids and polynucleotides. It is also called nucleotide sequence.	DNA Sequence,Nucleotide Sequence,RNA Sequence,DNA Sequences,Base Sequences,Nucleotide Sequences,RNA Sequences,Sequence, Base,Sequence, DNA,Sequence, Nucleotide,Sequence, RNA,Sequences, Base,Sequences, DNA,Sequences, Nucleotide,Sequences, RNA
D001665	Binding Sites	The parts of a macromolecule that directly participate in its specific combination with another molecule.	Combining Site,Binding Site,Combining Sites,Site, Binding,Site, Combining,Sites, Binding,Sites, Combining
D015265	Site-Specific DNA-Methyltransferase (Adenine-Specific)	An enzyme responsible for producing a species-characteristic methylation pattern on adenine residues in a specific short base sequence in the host cell DNA. The enzyme catalyzes the methylation of DNA adenine in the presence of S-adenosyl-L-methionine to form DNA containing 6-methylaminopurine and S-adenosyl-L-homocysteine. EC 2.1.1.72.	DNA Modification Methylases (Adenine-Specific),DNA-Adenine Methylases,Modification Methylases (Adenine-Specific),Site-Specific Methyltransferases (Adenine-Specific),DNA Modification Methylases Adenine Specific,Modification Methylases (Adenine Specific),Site Specific Methyltransferases (Adenine Specific),DNA Adenine Methylases,Methylases, DNA-Adenine