Barbara Schellenberg

TL;DR: SylA defines a new class of proteasome inhibitors that includes glidobactin A (GlbA), a structurally related compound from an unknown species of the order Burkholderiales, for which it is shown that SylA irreversibly inhibits all three catalytic activities of eukaryotic proteasomes, thus adding prote asome inhibition to the repertoire of modes of action of virulence factors.

TL;DR: The lrx1 mutant phenotype is likely to be suppressed by changes in pectic polysaccharides or other cell wall components, and the rol1 mutations cause a change in the expression of a number of cell wall–related genes.

TL;DR: It is reported that syringolin A-producing bacteria are able to open stomata and, thus, counteract stomatal innate immunity in bean and Arabidopsis and demonstrates that proteasome activity is crucial for guard cell function.

TL;DR: The total synthesis of syringolin A and B was described, which together with enzyme kinetic and structural studies, allowed us to elucidate the structural determinants underlying the proteasomal subsite selectivity and binding affinity of syrbactins.

TL;DR: Cl cloning and functional analysis of a gene cluster involved in glidobactin synthesis from soil bacterial strain K481-B101 is reported, which according to its 16S rRNA sequence belongs to the Burkholderiales.