The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex

Cellulose synthase has two distinct functions: synthesis of the cellulose molecule (polymerization) and assembling the synthesized cellulose chains into the crystalline microfibril (crystallization). In the type I bacterial cellulose synthase (Bcs) complex, four major subunits - BcsA, BcsB, BcsC and BcsD - work in a coordinated manner. This study showed that the crystallization subunit BcsD interacts with the polymerization complex BcsAB in two modes: direct protein-protein interactions and indirect interactions through the product cellulose. We hypothesized that the former and latter modes represent the basal and active states of type I bacterial cellulose synthase, respectively, and this dynamic behaviour of the BcsD protein regulates the crystallization process of cellulose chains.

Automated summary

Cellulose synthase plays two distinct roles in the synthesis and crystallization of cellulose chains. The study reveals that the crystallization subunit BcsD interacts with the polymerization complex BcsAB through direct protein-protein interactions and indirect interactions mediated by the cellulose product. This dynamic behavior of BcsD protein regulates the cellulose crystallization process.