文献类型：期刊文献

英文题名：Heterologous assembly of red-type Rubisco and functional identification of chaperonin in Porphyridium purpureum

作者：Zhang, Wei[1,2];Sun, Liyun[1,2];Fan, Jianhua[1,2,3]

机构：[1]East China Univ Sci & Technol, State Key Lab Bioreactor Engn, 130 Meilong Rd, Shanghai 200237, Peoples R China;[2]East China Univ Sci & Technol, Dept Appl Biol, Shanghai 200237, Peoples R China;[3]Shihezi Univ, Sch Chem & Chem Engn, Shihezi 832003, Peoples R China

年份：2024

卷号：79

外文期刊名：ALGAL RESEARCH-BIOMASS BIOFUELS AND BIOPRODUCTS

收录：;WOS:【SCI-EXPANDED(收录号:WOS:001223147400001)】；

基金：This work is supported by the National Key Research and Development Program of Synthetic Biology 2019YFA0906300, Natural Science Foundation of Shandong Province ZR2019ZD17, Natural Science Foundation of Shanghai 23ZR1415100 and 21ZR1416400, and Funding Project of the State Key Laboratory of Bioreactor Engineering and Shanghai Collaborative Innovation Center for Biomanufacturing Technology. Thank for the suggestions by Professor Xiaobo Li from Westlake University with this letter.

语种：英文

外文关键词：Red-type Rubisco; Heterologous assembly; Expression; Chaperonin; Red algae; Diatom

摘要：In the natural growth process of organisms, Ribulose 1,5-diphosphate carboxylase/oxygenase (Rubisco) is the rate-limiting enzyme for carbon fixation in photosynthesis. However, its carboxylation is low and the reaction can be competitively inhibited by O 2 . Red-type Rubiscos are known with higher catalytic rates and CO 2 /O 2 specificity, but their incompatibility with chaperonins in the green lineage pose challenges for them to be assembled and accumulated in C3 plants. In this study, we systematically explored the factors and conditions required for heterologous accumulation Rubisco from Porphyridium purpureum and that from Phaeodactylum tricornutum . We found that P. purpureum Rubisco required less co-factors to be produced in Escherichia coli than the P. tricornutum needed. In addition, the amino acid sequences of the co-chaperonin Cpn10 and Cpn20 in P. purpureum were retrieved, and they can assist in GroEL to fold the red-type Rubisco large subunits in vitro and in E. coli . Heterogeneous system research on Rubisco assembly conditions are of great significance for humans to understand CO 2 fixation mechanism, improve crop yield and mitigate global climate change.