PRESS RELEASES
Please quote Nature Chemical Biology as the source of these items.
The April 2008 issue of Nature Chemical Biology is available online.
April 2008
Pass the acetyl, please
pp 232 - 234A method for adding 'acetyls' onto specific sites in proteins is reported online in Nature Chemical Biology this week.
Acetyls — small chemicals — are added onto many different proteins inside cells and are important for regulating processes including epigenetics and cellular signalling. In fact, the addition of acetyls to proteins happens so widely that it appears to be as important as phosphorylation in controlling cellular processes. However, the biological consequences of the 'acetylation' of proteins are relatively poorly understood because it has not been easy to make proteins with an acetyl at the right spot and study the effects.
Jason Chin and colleagues have created a method for putting acetyls onto specific positions in proteins inside Escherichia coli. This easy method for making acetylated proteins will open up many new opportunities to understand this important biological modification.
Cleaning up a mouldy hormone
pp 235 - 237Scientists have identified the structure of an important hormone in mould, according to a paper to be published online this week in Nature Chemical Biology. This insight ends a 70-year search for the compound's shape and opens the door for biological studies of and treatment for the destructive Phytophthora fungi.
Hormone alpha1 was previously identified as an important molecule that causes Phytophthora moulds to become oospores — a protective form that allows the mould to survive for a long time in adverse conditions. However, because the compound is difficult to isolate and has a complex structure that cannot be assigned by standard methods, it has not been possible to conclusively determine the structure.
In a collaborative effort, Arata Yajima and colleagues and Yong Qin and colleagues have now determined two synthetic pathways to make the compound, and with the assistance of Jianhua Qi and colleagues, have also determined which of several structural possibilities is the true hormone. Knowing what this molecule looks like will help scientists trying to study the mould and may assist in finding drugs to combat these problematic microorganisms.
The not-so-sweet side of malaria
pp 238 - 240A chip that can be used to understand how people respond to toxic malarial sugars is described in a paper published online this week in Nature Chemical Biology. The chip, and the information it provides, could be used to aid future efforts in creating effective antimalarial vaccines.
The malarial parasite, Plasmodium falciparum, makes a large amount of sugars called GPIs. Rather than being 'sweet', these GPI sugars are quite toxic, and a vaccine against them could protect people from getting malaria. However, because it is not easy to obtain pure samples of these complicated sugars, it has been difficult to determine exactly which GPI sugars might be most useful for a vaccine.
Using very pure samples made chemically, Peter Seeberger and colleagues attached malarial GPI sugars to a glass slide to create a GPI chip. Using this chip, the authors looked at the antibodies that were made by people before and after exposure to malaria. After malarial exposure, people had more antibodies to only very specific GPI sugars.
Receptor crystallization speeds up
pp 241 - 247Scientists have discovered a method for generating structures of proteins that are difficult to work with, according to a paper to be published online this week in Nature Chemical Biology. The technique has major implications for drug design and in understanding the biology of these biomolecules.
Many natural small molecules are sensed in the cell by protein receptors; drugs that imitate these small molecules have the potential to prevent this 'sensing' or be 'sensed' themselves. However, the instability of the receptors means that it's very difficult to learn about the three-dimensional structure of the proteins, which also makes it much harder to understand the way small molecules interact with the proteins or to design new molecules.
Kendall Nettles and colleagues have now discovered that introduction of mutations that keep the proteins in one configuration or another provides a much needed boost in generating structures. Use of this method allowed the authors to learn about the specific contacts between the oestrogen receptor and several known small molecules.
Genetically encoding Nε-acetyllysine in recombinant proteins
pp 232 - 234Heinz Neumann, Sew Y Peak-Chew and Jason W Chin
Published online: 17 February 2008 | doi 10.1038/nchembio.73
Synthesis and absolute configuration of hormone α1
pp 235 - 237Arata Yajima, Yong Qin, Xuan Zhou, Naoki Kawanishi, Xue Xiao, Jue Wang, Dan Zhang, Yi Wu, Tomoo Nukada, Goro Yabuta, Jianhua Qi, Tomoyo Asano and Youji Sakagami
Published online: 24 February 2008 | doi 10.1038/nchembio.74
Synthetic GPI array to study antitoxic malaria response
pp 238 - 240Faustin Kamena, Marco Tamborrini, Xinyu Liu, Yong-Uk Kwon, Fiona Thompson, Gerd Pluschke and Peter H Seeberger
Published online: 2 March 2008 | doi 10.1038/nchembio.75
NFκB selectivity of estrogen receptor ligands revealed by comparative crystallographic analyses
pp 241 - 247Kendall W Nettles, John B Bruning, German Gil, Jason Nowak, Sanjay K Sharma, Johnnie B Hahm, Kristen Kulp, Richard B Hochberg, Haibing Zhou, John A Katzenellenbogen, Benita S Katzenellenbogen, Younchang Kim, Andrzej Joachimiak & Geoffrey L Greene
Published online: 16 March 2008 | doi 10.1038/nchembio.76
