Genetics & Molecular Biology

Reporting in the Journal of Biological Chemistry, an international team of researchers has determined the structure of 14α-Demethylase (14DM), an enzyme essential to the survival of the protozoan parasites that cause sleeping sickness, Chagas disease and leishmaniasis. They say this new information provides the first up-close look at the busy enzyme and, perhaps more importantly, shows how one compound in particular prevents it from conducting business as usual.

The team chose to attack the parasite's enzyme known as 14DM because it has a counterpart in fungi, which cause athlete's foot and ringworm, and such fungal infections are commonly treated with drugs that prevent 14DM from making ergosterol, a sterol required for membrane synthesis.
What will geneticists and molecular cell biologists be doing in 2020? 10 years ago, genomic technologies like DNA microarrays were just beginning to change the way molecular biologists worked, and the draft sequence of the human genome was a year from publication. Over the next decade, genomics, in the form of high-throughput tools, and large sequence databases, completely transformed the day-to-day work of just about everyone in the basic biomedical sciences.
Cancer-initiating cells that launch glioblastoma multiforme, the most
lethal type of brain tumor, also suppress an immune system attack on
the disease, scientists from The University of Texas M. D. Anderson
Cancer Center report in a paper featured on the cover of the Jan. 15
issue of Clinical Cancer Research.(1)

Glioblastoma Muliforme

Earlier this week I argued that biological systems posses dynamical properties that are biologically important, and understandable primarily through mathematical modeling. As an example, I discussed a paper that explored the advantages of double positive feedback loops in bistable switches.

I glossed over the math behind the model because of space and time constraints. (Constraints on a blog, you wonder? Well, I ran out of time, and once a blog post gets beyond 1000 words, the number people who read it to completion probably drops exponentially for every word over 1000.)
Using proteosome inhibitors to trick cells into producing a chaperone protein called Hsp70 may be one way of enhancing the natural ability of cells to restore their own mutant proteins. Researchers at the Fox Chase Cancer Center say the discovery may help treat certain debilitating – or even fatal – genetic diseases.

Scientists have just identified several molecules capable of reversing the brain abnormalities of Parkinson’s disease (PD), while also uncovering new clues for its origin in a study just published in the journal Disease Models and Mechanisms (1). PD is characterised by abnormal deposits of a brain protein called alpha-synuclein throughout the damaged brain regions, but exactly what they do there is not clear.


Why should we bother building mathematical models of biological systems? Scientists from other fields might wonder why one would as such a question - physicists, climate scientists, economists, engineers, and chemists all use mathematical models to understand the world.

Some biologists do too - individual proteins are studied with quantum mechanical models by biophysicists, enzyme reactions are modeled by biochemists, physiologists have mathematical models of the circulatory system, and population geneticists model the evolution of gene frequencies in populations.
Why are some people willing to take risks by gambling on "longshot" payoffs while, on the other hand, taking the opposite tack by buying insurance to reduce their risks? An international team of economists and molecular geneticists says the answer can be found in our genetic makeup.

In an article recently published online in PLoS ONE, researchers combined the tools of experimental economics and molecular genetics to examine the role of a well-characterized
gene, monoamine oxidase A (MAOA), in predicting whether subjects are more likely to buy the lottery or insurance (or both) under well-controlled laboratory conditions.
A molecule called Alda-1 can repair Aldehyde dehydrogenase 2 (ALDH2), an often defective alcohol metabolism enzyme that affects an estimated 1 billion people worldwide, according to research published Jan. 10 in the advance online edition of Nature Structural and Molecular Biology. The findings suggest the possibility of a treatment to reduce the health problems associated with the enzyme defect.

After alcohol is consumed, it is metabolized into acetaldehyde, a toxic chemical that causes DNA damage.  Aldehyde dehydrogenase 2 (ALDH2) is the main enzyme responsible for breaking down acetaldehyde into acetate, a nontoxic metabolite in the body.  It also removes other toxic aldehydes that can accumulate in the body.