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Structure of acid deoxyribonuclease
Armando Varela-Ramirez1, Jan Abendroth2,3, Adrian A Mejia1
1Department of Biological Sciences, Border Biomedical Research Center, The University of Texas at El Paso, El Paso, TX 79968, USA.
Nucleic Acids Research
|April 4, 2017
Summary
Burkholderia thailandensis deoxyribonuclease II (DNase II) functions optimally at low pH without metal ions. Structural analysis reveals a dimeric form with similarities to other enzymes, offering insights into DNase II
Area of Science:
- Biochemistry
- Structural Biology
- Enzymology
Background:
- Deoxyribonuclease II (DNase II), or acid deoxyribonuclease, is active in acidic environments like lysosomes.
- DNase II has been found in bacteria, suggesting horizontal gene transfer.
Purpose of the Study:
- To characterize the biochemical and structural properties of recombinant Burkholderia thailandensis DNase II.
- To investigate the catalytic mechanism and structural similarities of bacterial DNase II.
Main Methods:
- Recombinant protein expression and purification.
- Enzyme activity assays at varying pH and ionic conditions.
- X-ray crystallography for structural determination.
Main Results:
- B. thailandensis DNase II exhibits optimal activity at low pH and is independent of divalent metal ions.
- The crystal structure reveals a dimeric quaternary structure capable of DNA binding.
- The monomeric fold is similar to phospholipase D, phosphatidylserine synthase, and tyrosyl-DNA phosphodiesterase.
Conclusions:
- B. thailandensis DNase II shares functional and structural characteristics with eukaryotic DNase II.
- Conserved catalytic residues suggest a conserved enzymatic mechanism across different DNase II families.
- The study provides atomic-level insights into the structure and function of bacterial DNase II.