Interaction of the EcoDam methyltransferase with synthetic oligodeoxyribonucleotides

Gene

Volumn 74, Issue 1, 1988, Pages 67-69

  Buryanov, Y I ^b   Zinoviev, V V ^a   Gorbunov, Yu A ^a   Tuzikov, F V ^a   Rechkunova, N I ^a   Malygin, E G ^a   Bayev, A A ^b  

^a STATE RESEARCH CENTER OF VIROLOGY AND BIOTECHNOLOGY VECTOR   (Russian Federation)

^b SKRYABIN INSTITUTE OF BIOCHEMISTRY AND PHYSIOLOGY OF MICROORGANISMS   (Russian Federation)

Author keywords

DNA methyltransferase; enzyme dimerization; methylatable substrate structure; recognition site defects

Indexed keywords

DNA METHYLTRANSFERASE; METHYLTRANSFERASE; OLIGODEOXYRIBONUCLEOTIDE;

HEREDITY; NONHUMAN; PRIORITY JOURNAL;

BACTERIAL PROTEINS; BASE SEQUENCE; ESCHERICHIA COLI; METHYLATION; MOLECULAR SEQUENCE DATA; NUCLEIC ACID CONFORMATION; OLIGODEOXYRIBONUCLEOTIDES; PROTEIN CONFORMATION; SITE-SPECIFIC DNA-METHYLTRANSFERASE (ADENINE-SPECIFIC); SUBSTRATE SPECIFICITY; X-RAY DIFFRACTION;

EID: 0024247377     PISSN: 03781119     EISSN: None     Source Type: Journal    
DOI: 10.1016/0378-1119(88)90253-3     Document Type: Article

References (4)

1. The isolation and characterization of the Escherichia coli DNA adenine methylase (dam) gene
2. Does the DNA methylase EcoDam pair nucleotide sequences to form site-specific duplexes?
3. Escherichia coli dam methylase. Physical and catalytic properties of the homogeneous enzyme
4. Application of small angle x-ray scattering for the investigation of substrate-induced changes of methylase state