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

FEBS Letters

article

Tatsuya Kondo¹  Yui Nakamura²  Shingo Nojima²  Min Yao²  Tomoya Imai¹ 

[1] Research Institute for Sustainable Humanosphere ,(RISH), Kyoto University;Faculty of Advanced Life Science, Hokkaido University

关键词: cellulose;    cellulose synthase;    membrane protein complex;    protein–protein interaction;   

DOI  :  10.1002/1873-3468.14495

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown