Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

Scientists reveal DNA-enzyme interaction with first ever real time footage

17.09.2007
For the first time scientists have been able to film, in real time, the nanoscale interaction of an enzyme and a DNA strand from an attacking virus. Researchers from the University of Cambridge have used a revolutionary Scanning Atomic Force Microscope in Japan to produce amazing footage of a protective enzyme unravelling the DNA of a virus trying to infect a bacterial host.

The film is available to view at: http://www.bbsrc.ac.uk/media/pressreleases/video_enzyme_unravelling_dna.html

The research, funded by the Biotechnology and Biological Sciences Research Council (BBSRC), will improve our understanding of how enzymes interact with DNA at a nanoscale but also has marked implications for scientists studying DNA repair, and could help in the search for cancer treatments.

Working with researchers in Edinburgh, Japan and India, the Cambridge team used a state-of-the-art microscope, only three of which exist in the world, and a technique known as fast-scan atomic force microscopy (AFM). Before now, scientists could only make assumptions as to how proteins and DNA interact based on indirect evidence but this new window on a fundamental biological process gives them the opportunity to view how the interaction actually occurs.

... more about:
»DNA »Interaction »Real »interact

Dr Robert Henderson, who led the Cambridge research, explains: "This is the first time that such a process has been seen in real time. To be able see these nano-mechanisms as they are really happening is incredibly exciting. We can actually see the enzyme 'threading' through a loop in the virus's DNA in order to lock on to and break it, a process known as DNA cleavage.

"The microscope and new techniques give us a clear view of the molecular interactions between proteins and DNA that we could only previously interpret indirectly. The indirect methods require scientists to make assumptions to interpret their data, and video footage like this can help to provide a more direct understanding of what is really happening.

"Standard technology for filming on this scale can only produce one image frame every 8 minutes. However, our new work allows one frame per 500 - or fewer, milliseconds."

The footage shows a bacterial type III restriction enzyme attaching itself to the DNA of a virus, in order to break the DNA before the virus has the chance to infect the bacterium. However, this could also provide a model for understanding how other enzymes and DNA, in any type of organism, including humans, interact.

"This helps us understand how enzymes recognise which bit of a DNA strand to latch onto, which is important in understanding how proteins repair damaged DNA. In the long term, this could help in the search for cancer treatments, as cancer sometimes occurs where DNA is damaged but enzymes do not behave correctly in order to repair it."

Steve Visscher, interim BBSRC Chief Executive, said: "BBSRC strongly supports the development of new tools and resources and this study clearly highlights the significance of cutting-edge technologies to bioscience research. It is essential that bioscientists can draw upon technologies from the physical and engineering sciences to improve their understanding of biological processes."

Michelle Kilfoyle | alfa
Further information:
http://www.bbsrc.ac.uk
http://www.bbsrc.ac.uk/media/pressreleases/video_enzyme_unravelling_dna.html

Further reports about: DNA Interaction Real interact

More articles from Life Sciences:

nachricht Climate Impact Research in Hannover: Small Plants against Large Waves
17.08.2018 | Leibniz Universität Hannover

nachricht First transcription atlas of all wheat genes expands prospects for research and cultivation
17.08.2018 | Leibniz-Institut für Pflanzengenetik und Kulturpflanzenforschung

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

Die letzten 5 Focus-News des innovations-reports im Überblick:

Im Focus: Color effects from transparent 3D-printed nanostructures

New design tool automatically creates nanostructure 3D-print templates for user-given colors
Scientists present work at prestigious SIGGRAPH conference

Most of the objects we see are colored by pigments, but using pigments has disadvantages: such colors can fade, industrial pigments are often toxic, and...

Im Focus: Unraveling the nature of 'whistlers' from space in the lab

A new study sheds light on how ultralow frequency radio waves and plasmas interact

Scientists at the University of California, Los Angeles present new research on a curious cosmic phenomenon known as "whistlers" -- very low frequency packets...

Im Focus: New interactive machine learning tool makes car designs more aerodynamic

Scientists develop first tool to use machine learning methods to compute flow around interactively designable 3D objects. Tool will be presented at this year’s prestigious SIGGRAPH conference.

When engineers or designers want to test the aerodynamic properties of the newly designed shape of a car, airplane, or other object, they would normally model...

Im Focus: Robots as 'pump attendants': TU Graz develops robot-controlled rapid charging system for e-vehicles

Researchers from TU Graz and their industry partners have unveiled a world first: the prototype of a robot-controlled, high-speed combined charging system (CCS) for electric vehicles that enables series charging of cars in various parking positions.

Global demand for electric vehicles is forecast to rise sharply: by 2025, the number of new vehicle registrations is expected to reach 25 million per year....

Im Focus: The “TRiC” to folding actin

Proteins must be folded correctly to fulfill their molecular functions in cells. Molecular assistants called chaperones help proteins exploit their inbuilt folding potential and reach the correct three-dimensional structure. Researchers at the Max Planck Institute of Biochemistry (MPIB) have demonstrated that actin, the most abundant protein in higher developed cells, does not have the inbuilt potential to fold and instead requires special assistance to fold into its active state. The chaperone TRiC uses a previously undescribed mechanism to perform actin folding. The study was recently published in the journal Cell.

Actin is the most abundant protein in highly developed cells and has diverse functions in processes like cell stabilization, cell division and muscle...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

VideoLinks
Industry & Economy
Event News

LaserForum 2018 deals with 3D production of components

17.08.2018 | Event News

Within reach of the Universe

08.08.2018 | Event News

A journey through the history of microscopy – new exhibition opens at the MDC

27.07.2018 | Event News

 
Latest News

Smallest transistor worldwide switches current with a single atom in solid electrolyte

17.08.2018 | Physics and Astronomy

Robots as Tools and Partners in Rehabilitation

17.08.2018 | Information Technology

Climate Impact Research in Hannover: Small Plants against Large Waves

17.08.2018 | Life Sciences

VideoLinks
Science & Research
Overview of more VideoLinks >>>