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Modification methylase M.Sau3239I from Streptomyces aureofaciens 3239

E Zelinková1, M Paulícek, J Zelinka

  • 1Institute of Molecular Biology, Slovak Academy of Sciences, Bratislava, Czechoslovakia.

FEBS Letters
|October 1, 1990
PubMed

Insights

Researchers purified the modification methylase M.Sau3239I from Streptomyces aureofaciens. This enzyme methylates adenine in DNA, protecting it from restriction endonuclease R.Sau3239I cleavage.

Area of Science:

  • Molecular Biology
  • Enzymology
  • Microbial Genetics

Background:

  • Restriction-modification systems are crucial for bacterial defense and genome regulation.
  • DNA methylation plays a key role in protecting host DNA from restriction enzymes.

Purpose of the Study:

  • To detect and partially purify the modification methylase M.Sau3239I from Streptomyces aureofaciens.
  • To characterize the enzymatic activity and recognition sequence of M.Sau3239I.

Main Methods:

  • Chromatography techniques, including phosphocellulose and Heparin-Sepharose, were employed for enzyme purification.
  • Enzyme activity was assessed by its ability to methylate DNA and confer protection against restriction digestion.

Main Results:

  • The modification methylase M.Sau3239I was successfully detected and partially purified.
  • The enzyme was identified as catalyzing the methylation of adenine to N-6-methyladenine.
  • The specific recognition sequence for M.Sau3239I was determined to be 5'-CTCGmAG-3'.

Conclusions:

  • M.Sau3239I is a DNA modification methylase from Streptomyces aureofaciens.
  • The enzyme's activity involves methylation at adenine within the 5'-CTCGmAG-3' sequence.
  • This methylation event confers protection against the cognate restriction endonuclease R.Sau3239I.

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