Data-Independent Acquisition (DIA) Is Superior for High Precision Phospho-Peptide Quantification in .

The dynamic interplay of signaling networks in most major cellular processes is characterized by the orchestration of reversible protein phosphorylation. Consequently, analytic methods such as quantitative phospho-peptidomics have been pushed forward from a highly specialized edge-technique to a powerful and versatile platform for comprehensively analyzing the phosphorylation profile of living organisms. Despite enormous progress in instrumentation and bioinformatics, a high number of missing values caused by the experimental procedure remains a major problem, due to either a random phospho-peptide enrichment selectivity or borderline signal intensities, which both cause the exclusion for fragmentation using the commonly applied data dependent acquisition (DDA) mode.

Controllable Bypass Suppression in Magnaporthe oryzae.

Evolutionary adaptation of living organisms is commonly thought to be the result of processes that have taken place over long periods of time. By contrast, we found that the filamentous rice blast fungus Magnaporthe oryzae rapidly suppresses the osmosensitive "loss of function" (lof) phenotype in knockout mutants of the high-osmolarity glycerol (HOG) pathway. That suppression occurs highly reproducibly after 4 weeks of continuous growth upon salt stress.

The Molecular Mechanism of Fludioxonil Action Is Different to Osmotic Stress Sensing.

The group III two-component hybrid histidine kinase MoHik1p in the filamentous fungus is known to be a sensor for external osmotic stress and essential for the fungicidal activity of the phenylpyrrole fludioxonil. The mode of action of fludioxonil has not yet been completely clarified but rather assumed to hyperactivate the high osmolarity glycerol (HOG) signaling pathway. To date, not much is known about the detailed molecular mechanism of how osmotic stress is detected or fungicidal activity is initiated within the HOG pathway.