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

当前位置： X-MOL 学术 › FEBS Lett. › 论文详情

Our official English website, www.x-mol.net, welcomes your feedback! (Note: you will need to create a separate account there.)

The BcsD subunit of type I bacterial cellulose synthase interacts dynamically with the BcsAB catalytic core complex
FEBS Letters ( IF 3.0 ) Pub Date : 2022-09-14 , DOI: 10.1002/1873-3468.14495
Tatsuya Kondo ₁ , Yui Nakamura ₂ , Shingo Nojima ₂ , Min Yao ₂ , Tomoya Imai ₁

Affiliation

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.

中文翻译：

I 型细菌纤维素合酶的 BcsD 亚基与 BcsAB 催化核心复合物动态相互作用

纤维素合酶具有两个截然不同的功能：纤维素分子的合成（聚合）和将合成的纤维素链组装成结晶微纤维（结晶）。在 I 型细菌纤维素合酶 (Bcs) 复合物中，四个主要亚基 - BcsA、BcsB、BcsC 和 BcsD - 以协调的方式工作。该研究表明，结晶亚基 BcsD 以两种模式与聚合复合物 BcsAB 相互作用：直接蛋白质-蛋白质相互作用和通过产物纤维素的间接相互作用。我们假设前者和后者模式分别代表 I 型细菌纤维素合酶的基础和活性状态，并且 BcsD 蛋白的这种动态行为调节纤维素链的结晶过程。

更新日期：2022-09-14

点击分享查看原文

点击收藏

阅读更多本刊新发论文本刊介绍/投稿指南