News

no stress with pARG

In a study published in Mol Cell Proteomics, we report a mass spectrometric approach optimized for monitoring phospho-arginine, a chemically demanding protein modification. The improved methodology allowed us to quantitatively evaluate the pArg proteome under certain conditions and finally, to reveal the impact of protein arginine phosphorylation in orchestrating the bacterial stress response. more »

VBC PhD Award - Doris

Well deserved indeed :-) for Doris' great work on the UNC-45 chaperone (performed in close collaboration with Linn) leading to the discovery of a myosin assembly line. more »

RIP RIP Hurra

CtpB ring with its gated protease tunnel published in CELL. Indeed, it took quite some time to come to this stage, as first diffracting crystals were obtained in 2007. Overall, we were lucky that CtpB has lysozyme-like crystallization properties. Having seen the protease in distinct conformations allowed us to delineate its regulatory mechanism in great detail, as also illustrated in the protease-at-work movie section. more »

2013 Lab Retreat in Prague

One day science, one day culture and a short stop in the Staropramen brewery ... not the worst ingredients for a productive brainstorming session. From 6th-9th October, we had lively discussions about best recipes to dissect our dear protease and chaperone machines and to find the pArg needle in the proteome haystack. more »

PAPalaPAK

Identification and characterization of a phospo-arginine phosphatase (PAP) has been published in CELL REPORTS. Nice example that also small protein structures can be extremely thrilling – this time showing how a single, innocent residue near the active site turns out to be key in determining substrate specificity among protein phosphatases. Apparently, we have a PAP/PAK (YwlE phosphatase/McsB kinase) couple controlling protein arginine phosphorylation in bacteria. more »