Histone chaperones are key players involved in maintaining histone stability and dynamics in the cell. On pages 476–489, Das, et al. discuss the structural, biophysical and biochemical information on histone chaperones that is beginning to shape a new understanding of the integrated mechanisms of action for this important family of proteins. The cover shows an illustration of a histone chaperone-guided nucleosome assembly funnel. Histone chaperones ensure an ordered nucleosomal assembly pathway and prevent histones from being trapped in local minima during the process. The histone proteins are shown as space filling models with the histone H2A–H2B dimer in red, H3 in blue and H4 in green. The histone chaperones Asf1, RbAp46, and Chz1 are illustrated in a cartoon ribbon mode colored in cyan. Design by Mair Churchill.

The 2010 meeting in the Exciting Biologies Series
October 7-9, 2010
Sentosa Island, Singapore
Abstracts Due: July 7, 2010
Registration Deadline: August 6th
Learn More | Register
OzBio 2010 : The Molecules of Life - from Discovery to Biotechnology
Incorporating the 12th IUBMB, 21st FAOBMB and ComBio2010 Conferences
Sept 26 - Oct 1 2010, Melbourne Australia
http://www.asbmb.org.au/ozbio2010/
info@ozbio2010.com
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The histone shuffle: histone chaperones in an energetic dance In this Feature Review, Das, Tyler and Churchill discuss how biochemistry and structural biology have provided insights into how histone chaperones direct DNA replication, repair and transcription. *FREE DOWNLOAD* |
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Mitochondrial ROS regulate cellular signaling and dictate biological outcomes Accumulating evidence points to numerous cellular roles for reactive oxygen species. In this Review, Hamanaka and Chandel outline the regulated production of mitochondrial ROS and discuss the many cellular processes that are affected by their activity.
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When proteomics meets structural biology Although we have high resolution structures for many monomeric proteins and 'simple' complexes, large protein assemblies provide unique challenges to structural biologist. In this Review, Zhou and Robinson discuss how proteomics can be used in conjunction with low resolution structures can provide new insights into the functions of cellular machines.
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Also in this issue:
Where does amantadine bind to the influenza virus M2 proton channel?
JNK1: roles in metabolic regulation of insulin resistance
The carboxy terminal domain of RNA polymerase II and alternative splicing
The 3D structures of VDAC represent a native conformation
![]() | Through cleaving their target proteins, proteases direct numerous cellular pathways. Cleavage can result in activation or degradation, and can be important for triggering complex signaling pathways. Moreover, pathogens utilize proteolysis to attack (or hijack) host cells. How these diverse proteins function, and the outcomes of their action, has major implications for our approach to treating human disease.
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TiBS publishes papers online ahead of the print issue. Here are some of the latest:
| Barth and Imhof Fast signals and slow marks: the dynamics of histone modifications | Scherz-Shouval and Elazar Regulation of autophagy by ROS: physiology and pathology | |
| Stewart Nuclear export of mRNA | Kozlov et al. Protein-driven membrane stresses in fusion and fission | |
| Cross et al. Influence of solubilizing environments on membrane protein structures | Tennen and Chua Chromatin regulation and genome maintenance by mammalian SIRT6 |
These are the five most downloaded papers for the 30 days preceding September 9, 2010. See full list of most read articles