NMR to elucidate protein-DNA interaction

Determining exactly how proteins connect with specific DNA sequences in human cells has eluded researchers and scientists for years. While it has been possible to record the speed at which a protein could bond with DNA, little was known about how proteins located and connected with a specific pattern of DNA to allow genes to express themselves in the form of traits such as facial appearance, hair and eye color or behaviors.

In the July 16 issue of the journal Science, Rutgers-Newark chemistry professor Babis Kalodimos offers a solution to this puzzle in his paper, “Structure and Flexibility Adaptation in Nonspecific and Specific Protein-DNA Complexes.” Kalodimos’ findings may be the clue researchers need to develop future methods to inhibit the expression of certain genes that may pre-dispose individuals to harmful diseases such as cancer and Alzheimer’s disease.

Through the use of the nuclear magnetic resonance (NMR) spectroscopy, Kalodimos and his co-workers were able to determine how proteins slide along the lengthy strands forming the helix structure of DNA until they reach their intended destination – a specific DNA sequence. More important, they illustrated in detail how proteins single out their partner DNA out of millions of non-functional ones.

To better understand the scope of the question facing researchers, consider that billions of DNA codes exist within an individual’s genetic make-up and the protein must work its way through millions of non-specific DNA sequences in order to locate the correct connection.

DNA (Deoxyribonucleic acid) is a chemical structure that forms chromosomes. Structurally, DNA is a double helix made up of two strands of genetic material spiraled around each other. Each strand contains a sequence of bases (also called nucleotides). A base is one of four chemicals (adenine, guanine, cytosine and thymine). The two strands of DNA are connected at each base, but each base will only bond with one other specific base. For example, Adenine (A) will only bond with thymine (T), and guanine (G) will only bond with cytosine (C).

“We know that any protein binds first with any irrelevant DNA sequence, but the interaction is weak. It searches for the correct sequence by sliding along the DNA until it can bind with a specific DNA sequence and form a complex,” Kalodimos explained. “This helps us begin to complete the story of how proteins and DNA find each other in a very fast and accurate way. It provides us with a classical model for understanding protein-DNA interaction and offers valuable information about how transcription can be modulated at the gene level.”

Media Contact

Peter Haigney EurekAlert!

Weitere Informationen:

http://www.rutgers.edu

Alle Nachrichten aus der Kategorie: Life Sciences

Articles and reports from the Life Sciences area deal with applied and basic research into modern biology, chemistry and human medicine.

Valuable information can be found on a range of life sciences fields including bacteriology, biochemistry, bionics, bioinformatics, biophysics, biotechnology, genetics, geobotany, human biology, marine biology, microbiology, molecular biology, cellular biology, zoology, bioinorganic chemistry, microchemistry and environmental chemistry.

Zurück zur Startseite

Kommentare (0)

Schreib Kommentar

Neueste Beiträge

How Stable is the Antarctic Ice Sheet?

Scientists from Heidelberg University investigate which factors determine the stability of ice masses in East Antarctica. As temperatures rise due to climate change, the melting of polar ice sheets is…

Smart sensors for future fast charging batteries

European project “Spartacus” launched Faster charging, longer stability of performance not only for electric vehicles but also for smartphones and other battery powered products. What still sounds like science fiction…

Small molecules control bacterial resistance to antibiotics

Antibiotics have revolutionized medicine by providing effective treatments for infectious diseases such as cholera. But the pathogens that cause disease are increasingly developing resistance to the antibiotics that are most…

Partners

By continuing to use the site, you agree to the use of cookies. more information

The cookie settings on this website are set to "allow cookies" to give you the best browsing experience possible. If you continue to use this website without changing your cookie settings or you click "Accept" below then you are consenting to this.

Close