DNA topoisomerase: Difference between revisions

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&nbsp;DNA topoisomerase plays an important role in breaking the phosphodiester bond by binding covalently onto the DNA backbone phosphate<ref>Alberts, BA, 2008. Molecular Biology of The Cell. 5th ed. New York: Garland Science.</ref>. It acts as a reversible nuclease. This whole process is a reversible one, whereby before the protein leaves, the phosphodiester bonds are re-made. There are two types of DNA topoisomerase, topoisomerase I and topoisomerase II<ref>Alberts, BA, 2008. Molecular Biology of The Cell. 5th ed. New York: Garland Science.</ref>.  
[[DNA|DNA]] topoisomerase&nbsp;plays an impotant role in breaking the [[Phosphodiester bond|phosphodiester bond]] by binding covalently onto the DNA backbone [[Phosphate|phosphate]]. It acst as a [[Reversible nuclease|reversible nuclease]]. This whole process is a reversible one, whereby before the [[Proteins|protein]] leaves, the phosophodiester bonds are re-made.&nbsp;There are two types of DNA topoisomerase, [[DNA topoisomerase I|topoisomerase I]] and [[DNA topoisomerase II|topoismerase II]]<ref>Alberts, BA, 2008. Molecular Biology of The Cell. 5th ed. New York: Garland Science.</ref>.  


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== '''Topoisomerase I'''  ==


=== Reference&nbsp;:  ===
Topoisomerase I catalyses the cleavage of the double stranded DNA by relaxing the supercoiled DNA. This process releases energy, as it is thermodynamically favourable <ref>Berg, J., Tymoczko, J., Stryer, L. and Berg, J. (2011). Student companion for Biochemistry, 7th edition, international edition. 1st ed. New York: W.H. Freeman.</ref>.<br>
 
== '''Topoisomerase II'''  ==
 
Topoisomerase II (also called gyrase) cleaves the double-stranded DNA by adding negative supercoils to DNA. Duplex DNA requires unrestricted rotation when&nbsp;replicating, so a swivel mechanism exists to prevent&nbsp;stress building up on the duplex further along and possibly&nbsp;inhibiting strand separation. This&nbsp;mechanism of relieving&nbsp;stress&nbsp;is facilitated by&nbsp;toposimerase II (gyrase). Its&nbsp;method of&nbsp;action involves cleaving dsDNA, rotating&nbsp;the ends of these broken strands, thereby relieving torsional stress, and re-joining the strands. &nbsp;&nbsp;This process hydrolyses [[ATP|ATP]] to produce the required energy <ref>Berg, J., Tymoczko, J., Stryer, L. and Berg, J. (2011). Student companion for Biochemistry, 7th edition, international edition. 1st ed. New York: W.H. Freeman.</ref>.<br>
 
=== Reference ===


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Latest revision as of 11:17, 19 November 2015

DNA topoisomerase plays an impotant role in breaking the phosphodiester bond by binding covalently onto the DNA backbone phosphate. It acst as a reversible nuclease. This whole process is a reversible one, whereby before the protein leaves, the phosophodiester bonds are re-made. There are two types of DNA topoisomerase, topoisomerase I and topoismerase II[1].

Topoisomerase I

Topoisomerase I catalyses the cleavage of the double stranded DNA by relaxing the supercoiled DNA. This process releases energy, as it is thermodynamically favourable [2].

Topoisomerase II

Topoisomerase II (also called gyrase) cleaves the double-stranded DNA by adding negative supercoils to DNA. Duplex DNA requires unrestricted rotation when replicating, so a swivel mechanism exists to prevent stress building up on the duplex further along and possibly inhibiting strand separation. This mechanism of relieving stress is facilitated by toposimerase II (gyrase). Its method of action involves cleaving dsDNA, rotating the ends of these broken strands, thereby relieving torsional stress, and re-joining the strands.   This process hydrolyses ATP to produce the required energy [3].

Reference

  1. Alberts, BA, 2008. Molecular Biology of The Cell. 5th ed. New York: Garland Science.
  2. Berg, J., Tymoczko, J., Stryer, L. and Berg, J. (2011). Student companion for Biochemistry, 7th edition, international edition. 1st ed. New York: W.H. Freeman.
  3. Berg, J., Tymoczko, J., Stryer, L. and Berg, J. (2011). Student companion for Biochemistry, 7th edition, international edition. 1st ed. New York: W.H. Freeman.