Shapes of 200 human GPCRs to be determined over next 5 years

http://news.sciencemag.org/biology/2014/10/giving-shapes-signaling-proteins?utm_campaign=email-news-latest&utm_source=eloqua

"Some 40% of all approved drugs target the proteins called G protein-coupled receptors (GPCRs), which relay signals across the cell membrane. But we know the 3D shapes of just 22 of the estimated 826 human GPCRs. This week, a trio of U.S. and Chinese academic institutions announced that they’ll join forces over the next 5 years with three pharmaceutical companies to determine the structures of 200 more."

Harris 2014 - A Caulobacter MreB mutant with irregular cell shape exhibits compensatory widening to maintain a preferred surface area to volume ratio

Sick cells with sick shapes: Leigh's paper is the essence of Sick Cell Shape Papes!

 

Modell et al. 2014 -- A DNA Damage-Induced, SOS-Independent Checkpoint Regulates Cell Division in Caulobacter crescentus

http://www.plosbiology.org/article/info:doi/10.1371/journal.pbio.1001977

Here's their author summary:
Cells have evolved sophisticated mechanisms for repairing their DNA and maintaining genome integrity. A critical aspect of the repair process is an arrest of cell cycle progression, thereby ensuring that cell division is not attempted before the genome has been repaired and fully duplicated. Our paper explores the molecular mechanisms that underlie the inhibition of cell division following DNA damage in the bacterium Caulobacter crescentus. For most bacteria, the primary, and only mechanism previously described involves the SOS response, in which DNA damage induces cleavage of the transcriptional repressor LexA, driving induction of a battery of genes that includes an inhibitor of cell division (sulA in E. coli and sidA in Caulobacter). Here, we report that Caulobacter cells have a second, SOS-independent damage response pathway that induces another division inhibitor, didA, which works together with sidA to block cell division following DNA damage. We also identify the damage-sensitive transcription factor responsible for inducing DidA. Finally, our study demonstrates that DidA and SidA inhibit cell division in an atypical manner. Many division inhibitors in bacteria appear to inhibit the protein FtsZ, which forms a ring at the site of cell division. DidA and SidA, however, target a trio of proteins, FtsW/I/N, that help synthesize the new cell wall that will separate the daughter cells (the septum). In sum, our work expands our understanding of how bacterial cells respond to DNA damage and the mechanisms by which they regulate cell division.

Theriot 2013 - Why are bacteria different from eukaryotes?

Julie soliliquizing.  Of interest to MreB people.

Chen -- Lattice light-sheet microscopy: Imaging molecules to embryos at high spatiotemporal resolution

New  in vivo imaging techinique

Sham - MurJ is the flippase of lipid-linked precursors for peptidoglycanbiogenesis Science 345, 220 (2014)

Clever assay to demonstrate that MurJ is the flippase of lipid II in E. coli.

Pilizota - Origins of Escherichia coli Growth Rate and Cell Shape Changes at High External Osmolality  Biophysical Journal Volume 107 October 2014 1962–1969

Further evidence that turgor doesn't drive growth in E. coli.