Forum for Science, Industry and Business

Sponsored by:     3M 
Search our Site:

 

’Ping-Pong’ mechanism seen in gene-controlling enzyme

30.10.2002


An enzyme that plays a pivotal role in controlling genes in yeast acts through a more versatile mechanism than was previously thought to be the case, according to a new study by researchers at The Wistar Institute.



Its mode of action is also distinct from that of other members of the vital enzyme family into which it falls, the scientists found. Because the human counterpart of the enzyme has been associated with certain forms of leukemia, this observation raises the possibility that drugs designed to specifically inhibit the enzyme might be useful in treating these cancers.

A report on the study appears in the November issue of Nature Structural Biology.


The enzyme studied, called Esa1, is one of a family of enzymes called HATs, which are responsible for relaxing, when appropriate, the tightly compacted DNA packaging that prevents genes from being accessed and activated most of the time. HATs do this by transferring an acetyl group from a coenzyme donor molecule to target proteins called histones that control the DNA packaging.

Other members of the enzyme family can accomplish this transfer only when all three components - the donor molecule, the enzyme, and the target - are in the same place. Esa1, on the other hand, is able to temporarily accept an acetyl group from the coenzyme donor before handing it off to the histone protein.

"This enzyme uses what we call a ping-pong mechanism," says Ronen Marmorstein, Ph.D., senior author on the study and an associate professor at The Wistar Institute. "First the acetyl molecule is transferred to the enzyme - ping - and then it goes from the enzyme to the histone protein - pong. It’s a different and more flexible way of getting your business done."

The time during which the enzyme is carrying the acetyl group is quite brief, Marmorstein notes, but he and his team were able to trap the moment in a crystallized form of the enzyme that they were then able to analyze more closely.

Earlier studies by Marmorstein’s group had shown that the molecular structure of the active region of the enzyme was nearly identical to the structures of the corresponding regions of other HATs. At that time, his team hypothesized that the mode of action of the enzymes might also be similar. The current study showed this not to be the case, however.

Franklin Hoke | EurekAlert!
Further information:
http://www.wistar.upenn.edu/

More articles from Life Sciences:

nachricht A novel socio-ecological approach helps identifying suitable wolf habitats
17.02.2017 | Universität Zürich

nachricht New, ultra-flexible probes form reliable, scar-free integration with the brain
16.02.2017 | University of Texas at Austin

All articles from Life Sciences >>>

The most recent press releases about innovation >>>

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

Im Focus: Breakthrough with a chain of gold atoms

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

In the field of nanoscience, an international team of physicists with participants from Konstanz has achieved a breakthrough in understanding heat transport

Im Focus: DNA repair: a new letter in the cell alphabet

Results reveal how discoveries may be hidden in scientific “blind spots”

Cells need to repair damaged DNA in our genes to prevent the development of cancer and other diseases. Our cells therefore activate and send “repair-proteins”...

Im Focus: Dresdner scientists print tomorrow’s world

The Fraunhofer IWS Dresden and Technische Universität Dresden inaugurated their jointly operated Center for Additive Manufacturing Dresden (AMCD) with a festive ceremony on February 7, 2017. Scientists from various disciplines perform research on materials, additive manufacturing processes and innovative technologies, which build up components in a layer by layer process. This technology opens up new horizons for component design and combinations of functions. For example during fabrication, electrical conductors and sensors are already able to be additively manufactured into components. They provide information about stress conditions of a product during operation.

The 3D-printing technology, or additive manufacturing as it is often called, has long made the step out of scientific research laboratories into industrial...

Im Focus: Mimicking nature's cellular architectures via 3-D printing

Research offers new level of control over the structure of 3-D printed materials

Nature does amazing things with limited design materials. Grass, for example, can support its own weight, resist strong wind loads, and recover after being...

Im Focus: Three Magnetic States for Each Hole

Nanometer-scale magnetic perforated grids could create new possibilities for computing. Together with international colleagues, scientists from the Helmholtz Zentrum Dresden-Rossendorf (HZDR) have shown how a cobalt grid can be reliably programmed at room temperature. In addition they discovered that for every hole ("antidot") three magnetic states can be configured. The results have been published in the journal "Scientific Reports".

Physicist Dr. Rantej Bali from the HZDR, together with scientists from Singapore and Australia, designed a special grid structure in a thin layer of cobalt in...

All Focus news of the innovation-report >>>

Anzeige

Anzeige

Event News

Booth and panel discussion – The Lindau Nobel Laureate Meetings at the AAAS 2017 Annual Meeting

13.02.2017 | Event News

Complex Loading versus Hidden Reserves

10.02.2017 | Event News

International Conference on Crystal Growth in Freiburg

09.02.2017 | Event News

 
Latest News

Tune your radio: galaxies sing while forming stars

21.02.2017 | Physics and Astronomy

Improved Speech Intelligibility and Automatic Speech-to-Text Conversion for Call Centers

21.02.2017 | Trade Fair News

36 big data research projects

21.02.2017 | Interdisciplinary Research

VideoLinks
B2B-VideoLinks
More VideoLinks >>>