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Related Concept Videos

DNA Helicases00:55

DNA Helicases

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DNA unwinding helicase enzymes are a type of motor protein. Motor proteins can translocate along filaments or polymers using energy generated from ATP hydrolysis. Helicases are involved in all the important cellular processes where DNA unwinding is required, such as DNA replication, repair, recombination, and transcription. They are present in all living organisms, but vary in their structure, function, and mechanism of action. For example, in prokaryotes, DnaB helicase binds and translocates...
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Topoisomerases are enzymes that relax overwound DNA molecules during various cell processes, including DNA replication and transcription. These enzymes regulate positive and negative DNA supercoiling without changing the nucleotide sequence. DNA overwinding in a clockwise direction results in positively supercoiled DNA, whereas underwinding in a counterclockwise direction produces negatively supercoiled DNA.
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Two structural features of the DNA molecule provide a basis for the mechanisms of heredity: the four nucleotide bases and its double-stranded nature. The Watson-Crick model of double-helical DNA structure, proposed in 1952, drew heavily upon the X-ray crystallography work of researchers Rosalind Franklin and Maurice Wilkins. Watson, Crick, and Wilkins jointly received the Nobel Prize in Physiology or Medicine for their work in 1962. Franklin was, controversially, excluded from the prize for...
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Synthesis of new DNA molecules is carried out by the enzyme DNA polymerase, which adds nucleotides on the daughter strand complementary to the template DNA strand. DNA polymerase has a higher affinity to add the correct base and ensures fidelity during DNA replication. Furthermore,  it exhibits proofreading activity during replication, using an exonuclease domain that cuts off incorrect nucleotides from the nascent DNA strand.
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Stretching Short Sequences of DNA with Constant Force Axial Optical Tweezers
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Optical Control of DNA Helicase Function through Genetic Code Expansion.

Ji Luo1, Muwen Kong2,3, Lili Liu3

  • 1Department of Chemistry, University of Pittsburgh, Pittsburgh, Pennsylvania, 15260, USA.

Chembiochem : a European Journal of Chemical Biology
|January 26, 2017
PubMed
Summary
This summary is machine-generated.

Researchers developed a light-activated DNA helicase (UvrD) for precise control over DNA repair. This optically triggered enzyme offers a new method for regulating DNA repair pathways and other ATPase functions.

Keywords:
DNA damagecaged compoundshelicaselight activationunnatural amino acids

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Area of Science:

  • Molecular Biology
  • Biochemistry
  • Genetics

Background:

  • Nucleotide excision repair (NER) removes diverse DNA lesions.
  • Bacterial UvrD helicase unwinds DNA for lesion removal.
  • Controlling NER activity is crucial for understanding DNA repair.

Purpose of the Study:

  • To create a light-controllable DNA helicase for conditional NER regulation.
  • To demonstrate optical switching of enzymatic activity in UvrD.
  • To establish a foundation for regulating ATP-dependent helicases.

Main Methods:

  • Site-specific incorporation of a genetically encoded hydroxycoumarin lysine into UvrD's ATP-binding pocket.
  • Development of a caged UvrD enzyme.
  • Functional assays to assess enzymatic activity and optical control.

Main Results:

  • The caged UvrD enzyme exhibited complete inactivity in functional assays.
  • Optically triggered UvrD showed restored enzymatic activity comparable to wild-type.
  • Demonstrated excellent OFF to ON switching of helicase activity via light activation.

Conclusions:

  • A light-activated UvrD helicase provides optical control over NER.
  • This methodology enables precise regulation of ATP-dependent helicase functions.
  • The approach is applicable for light-activation of various ATPases.