Litcius/Paper detail

E. coli Toxin YjjJ (HipH) Is a Ser/Thr Protein Kinase That Impacts Cell Division, Carbon Metabolism, and Ribosome Assembly

Fabio Lino Gratani, Till Englert, Payal Nashier, Peter Saß, Laura Czech, Niels Neumann, Sofía Doello, Petra Mann, Rudolf Blobelt, Siegfried Alberti, Karl Forchhammer, Gert Bange, Katharina Höfer, Boris Maček

2022mSystems15 citationsDOIOpen Access PDF

Abstract

Adaptation to growth condition is the key for bacterial survival, and protein phosphorylation is one of the strategies adopted to transduce extracellular signal in physiological response. In a previous work, we identified YjjJ, a putative kinase, as target of the persistence-related HipA kinase. Here, we performed the characterization of this putative kinase, complementing phenotypical analysis with SILAC-based phosphoproteomics and proteomics. We provide the first experimental evidence that YjjJ is a Ser/Thr protein kinase, having as primary protein substrates the ribosomal protein RpmE (L31) and the carbon storage regulator CsrA. We show that overproduction of YjjJ has a major influence on bacterial physiology, impacting DNA segregation, cell division, glycogen production, and ribosome assembly.

Topics & Concepts

Stable isotope labeling by amino acids in cell cultureBiologyPhosphoproteomicsKinaseCell biologyProtein kinase ACyclin-dependent kinase 2BiochemistryProtein phosphorylationProteomicsGeneBacterial Genetics and BiotechnologyRNA and protein synthesis mechanismsBacteriophages and microbial interactions