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Some bacteria have the remarkable ability to switch from a free-swimming, planktonic phase to coexistence in a complex biofilm. In this issue of NSMB, the structures of the ligand-bound c-di-GMP riboswitch give insight into some of the molecular processes linked to lifestyle changes but also suggest a potential avenue for applications that begs exploration.
The 2009 Nobel Prize for Physiology or Medicine goes to telomerase researchers, the Lasker Award to nuclear reprogramming pioneers, and crystallographers are awarded the Chemistry Nobel once again.
How does a transcription factor select a specific DNA response element given the presence of degenerate sequences? To date, this question has largely been viewed from the standpoint of DNA sequence variability and transcription factor binding affinity under steady-state conditions. Here we propose that to address this problem, it is also necessary to account for fluctuating cellular conditions. These lead to dynamic changes in the ensemble of protein (and DNA) conformational states via allosteric effects.
Manuscript peer reviewing is at the heart of the scientific system, but it seems that these duties are often not properly (if at all) recognized by universities, funding agencies or even the rest of the scientific community.
A recent survey revealed striking differences between the public and scientists' views of US scientific achievement and its societal benefits. This reinforces the fact that more must be done to effectively communicate with, educate and engage the public.
The US State Department promises to accelerate the visa process for foreign graduate students and postdoctoral researchers. That will be a welcome change.
The WD40 protein WDR5 is a core subunit of the human MLL and SET1 (hCOMPASS) histone H3 Lys4 (H3K4) methyltransferase complexes. Although initial studies suggested that WDR5 interacts with methylated H3K4 to catalyze Lys4 trimethylation, recent work has revealed that it binds an arginine-bearing motif in MLL1, promoting complex assembly and activity. These findings suggest that WDR5 functions as a peptidyl arginine–recognition factor that facilitates the assembly of hCOMPASS and other chromatin-modifying complexes.
The practice of origami dates from the 1600s, but this cannot compare to how long proteins have been evolving form and function. How proteins achieve their correct shape is the subject of this special Focus.
As we set off into the full swing of traveling for the globally oriented meeting season, it's worth also remembering the delights of local science consumption.
