The isolation and characterization of the Esherichia Coli DNA adenine methylase (dam) gene

Brooks, J. E., Blumenthal, R. M., Gingeras, T. R. (1983) The isolation and characterization of the Esherichia Coli DNA adenine methylase (dam) gene. Nucleic Acids Research, 11 (3). pp. 837-851. ISSN 03051048 (ISSN)

URL: http://www.ncbi.nlm.nih.gov/pubmed/6300769
DOI: 10.1093/nar/11.3.837

Abstract

The E coli dam (DNA adenine methylase) enxyne is known to nethylate the sequence GATC. A general nethod for cloning sequence-speoific DNA methylase genet was used to isolate the dam gene on a 1.14 kb fragment, inserted in the plasmid vector pBK322. Subsequent restriction mapping and subcloning experiments established a set of approximate boundaries of the gene. The nucleotide sequence of the dju gene was determined, and analysis of that sequence revealed a unique open reading frame which corresponded in length to that necessary to oode for a protein the sixe of dam. Amino acid conposition derived froa this sequence corresponds closely to the amino acid composition of the purified dam protein. Enxynatic and DNA:DNA hybridixation methods were used to investigate the possible presence of dasi genes in a variety of prokaryotlc organisms. © 1983 IRL Press Limited.

Item Type: Paper
Additional Information:
Uncontrolled Keywords: bacterial DNA DNA Cytosine 5 Methyltransferase DNA cytosine 5 methyltransferase methyltransferase restriction endonuclease amino acid sequence article bacterial gene enzymology Escherichia coli genetics isolation and purification molecular cloning nucleic acid hybridization nucleotide sequence plasmid structural gene Base Sequence Cloning, Molecular DNA Cytosine 5 Methyltransferase DNA Restriction Enzymes DNA, Bacterial Genes Bacterial Genes Structural Methyltransferases Plasmids
Subjects: bioinformatics > genomics and proteomics > genetics & nucleic acid processing > DNA, RNA structure, function, modification > DNA methylation
bioinformatics > genomics and proteomics > genetics & nucleic acid processing > protein structure, function, modification > protein types > enzymes
CSHL Authors:
Communities: CSHL labs > Gingeras lab
Depositing User: CSHL Librarian
Date Deposited: 14 Mar 2012 14:55
Last Modified: 31 Mar 2014 14:15
PMCID: PMC325756
Related URLs:
URI: http://repository.cshl.edu/id/eprint/25232

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