Effect of Rational Mutagenesis of Selected Cohesin Residues on the High-Affinity Cohesin-Dockerin Interaction

机译：选定黏蛋白残基的合理诱变对高亲和力黏蛋白-Dockerin相互作用的影响

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The high-affinity cohesin-dockerin interaction that dictates cellulosome assembly was probed by site-directed mutagenesis of suspected recognition residues on the cohesin domain. The involvement of two loops that flank the 8,3.6,5 β sheet of a cohesin domain of the cellulosomal scaffoldin from Clostridium thermocellum was examined by their partial replacement with analogous portions of a cohesin domain from Clostridium cellulolyticum. Similarly, several amino acids located on this β sheet were replaced with matching residues on the counter species cohesin. The dockerin-binding specificity of the cohesin was not altered by those mutations. However, the binding affinity of certain mutants significantly decreased, thus corroborating the notion that the dockerin-binding site stretches along this particular face of the cohesin molecule and that some of the mutated surface residues play a significant role in the binding process.

机译：通过对粘着蛋白结构域上的可疑识别残基进行定点诱变，探讨了指示纤维素体装配的高亲和力粘着蛋白-dockerin相互作用。通过用热解梭菌的粘着素结构域的类似部分部分替换，检查了两个环的侧面，这些环位于来自热纤梭菌的纤维素支架蛋白的粘连蛋白结构域的8,3.6,5β薄片的侧面。类似地，位于该β折叠上的几个氨基酸被对应物种黏附素上的匹配残基替换。这些突变不会改变粘着蛋白的dockerin结合特异性。但是，某些突变体的结合亲和力显着降低，从而证实了dockerin-结合位点沿着黏着分子的该特定面延伸并且某些突变的表面残基在结合过程中起着重要作用的观点。

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《ACS Symposium Series 889; American Chemical Society(ACS) National Meeting; 20030323-27; New Orleans,LA(US)》|2003年|P.194-206|共13页
会议地点 New OrleansLA(US)
作者
Tal Handelsman; Adva Mechaly; Yoav Barak; David Nakar; Raphael Lamed; Yuval Shoham; Edward A. Bayer;
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Department of Food Engineering and Biotechnology, Technion -Israel Institute of Technology, Haifa, Israel;

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正文语种 eng
中图分类生产过程;
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专利

1. Mapping by Site-Directed Mutagenesis of the Region Responsible for Cohesin-Dockerin Interaction on the Surface of the Seventh Cohesin Domain of Clostridium thermocellum CipA [J] . Isabelle Miras, Francis Schaeffer, Pierre Beguin, Biochemistry . 2002,第7期

机译：通过定点诱变在热纤梭菌CipA的第七个粘附素域表面上负责粘附素-泊坞蛋白酶相互作用的区域的映射。
2. Engineering a reversible, high-affinity system for efficient protein purification based on the cohesin-dockerin interaction. [J] . Karpol A, Kantorovich L, Demishtein A, Journal of molecular recognition: JMR . 2009,第2期

机译：设计一种可逆的，高亲和力的系统，用于基于cohesin-dockerin相互作用进行有效的蛋白质纯化。
3. Analysis of selective, high protein-protein binding interaction of cohesin-dockerin complex using biosensing methods [J] . Jeon S.D., Lee J.E., Kim S.J., Biosensors & Bioelectronics: The International Journal for the Professional Involved with Research, Technology and Applications of Biosensers and Related Devices . 2012,第Null期

机译：使用生物传感方法分析粘着蛋白-dockerin复合物的选择性高蛋白-蛋白结合相互作用
4. Effect of Rational Mutagenesis of Selected Cohesin Residues on the High-Affinity Cohesin-Dockerin Interaction [C] . Tal Handelsman, Adva Mechaly, Yoav Barak, American Chemical Society National Meeting . 2004

机译：选定的休谷蛋白残基合理诱变对高亲和力幼耳素相互作用的影响
5. Divergent cellulosome architecture in rumen bacteria: Structure and function studies in cohesin-dockerin complexes of Ruminococcus flavefaciens [D] . Gomes, Pedro Miguel Bule. 2017

机译：瘤胃细菌中不同的纤维素体结构：黄褐球菌黏附素-dockerin复合物的结构和功能研究
6. Crucial Roles of Single Residues in Binding Affinity Specificity and Promiscuity in the Cellulosomal Cohesin-Dockerin Interface [O] . Michal Slutzki, Dan Reshef, Yoav Barak, 2015

机译：单个残基在纤维素粘着蛋白-Dockerin界面的结合亲和力特异性和混杂中的重要作用
7. Species-scanning mutagenesis of the serotonin transporter reveals residues essential in selective, high-affinity recognition of antidepressants [O] . Ole V. Mortensen, Anders S. Kristensen, Ove Wiborg 2008

机译：血清素转运蛋白的物种扫描诱变揭示了在抗抑郁药的选择性，高亲和力识别方面所必需的残留物

Effect of Rational Mutagenesis of Selected Cohesin Residues on the High-Affinity Cohesin-Dockerin Interaction

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