The bacterial tyrosine kinase system CpsBCD governs the length of capsule polymers
Rei Nakamoto, Jeric Mun Chung Kwan, Jasmine Fei Li Chin, Hui Ting Ong, Josué Flores-Kim, Caroline Midonet, Michael S. VanNieuwenhze, Xue Li Guan, Lok‐To Sham
Abstract
accumulated low molecular weight CPS and lysed because of the lethal sequestration of the lipid carrier undecaprenyl phosphate, resulting in inhibition of peptidoglycan (PG) synthesis. CpsC interacts with CpsD and the polymerase CpsH. CpsD phosphorylation reduces the length of CPS polymers presumably by controlling the activity of CpsC. Finally, pulse-chase experiments reveal the spatiotemporal coordination between CPS and PG synthesis. This coordination is dependent on CpsC and CpsD. Together, our study provides evidence that BY-kinases regulate capsule polymer length by fine-tuning CpsC activity through autophosphorylation.