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Jang Min Park Baek-Rock Oh In Yeong Kang Sun-Yeon Heo Jeong-Woo Seo Seung-Moon Park Won-Kyung Hong Chul Ho Kim 《Journal of industrial microbiology & biotechnology》2017,44(7):1107-1113
A Bacillus sp. strain named BRC1 is capable of producing 2,3-butanediol (2,3-BD) using hydrolysates of the Jerusalem artichoke tuber (JAT), a rich source of the fructose polymer inulin. To enhance 2,3-BD production, we undertook an extensive analysis of the Bacillus sp. BRC1 genome, identifying a putative gene (sacC) encoding a fructan hydrolysis enzyme and characterizing the activity of the resulting recombinant protein expressed in and purified from Escherichia coli. Introduction of the sacC gene into Bacillus sp. BRC1 using an expression vector increased enzymatic activity more than twofold. Consistent with this increased enzyme expression, 2,3-BD production from JAT was also increased from 3.98 to 8.10 g L?1. Fed-batch fermentation of the recombinant strain produced a maximal level of 2,3-BD production of 28.6 g L?1, showing a high theoretical yield of 92.3%. 相似文献
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Leehyeon Kim Jiwon Heo Do Hoon Kwon Jin Seok Shin Se Hwan Jang ZeeYong Park Hyun Kyu Song 《Protein science : a publication of the Protein Society》2021,30(3):700
The N‐degron pathway determines the half‐life of proteins in both prokaryotes and eukaryotes by precisely recognizing the N‐terminal residue (N‐degron) of substrates. ClpS proteins from bacteria bind to substrates containing hydrophobic N‐degrons (Leu, Phe, Tyr, and Trp) and deliver them to the caseinolytic protease system ClpAP. This mechanism is preserved in organelles such as mitochondria and chloroplasts. Bacterial ClpS adaptors bind preferentially to Leu and Phe N‐degrons; however, ClpS1 from Arabidopsis thaliana (AtClpS1) shows a difference in that it binds strongly to Phe and Trp N‐degrons and only weakly to Leu. This difference in behavior cannot be explained without structural information due to the high sequence homology between bacterial and plant ClpS proteins. Here, we report the structure of AtClpS1 at 2.0 Å resolution in the presence of a bound N‐degron. The key determinants for α‐amino group recognition are conserved among all ClpS proteins, but the α3‐helix of eukaryotic AtClpS1 is significantly shortened, and consequently, a loop forming a pocket for the N‐degron is moved slightly outward to enlarge the pocket. In addition, amino acid replacement from Val to Ala causes a reduction in hydrophobic interactions with Leu N‐degron. A combination of the fine‐tuned hydrophobic residues in the pocket and the basic gatekeeper at the entrance of the pocket controls the N‐degron selectivity of the plant ClpS protein. 相似文献
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Benedetta Artegiani Lisa van Voorthuijsen Rik G.H. Lindeboom Daniëlle Seinstra Inha Heo Pablo Tapia Carmen López-Iglesias Daniel Postrach Talya Dayton Rurika Oka Huili Hu Ruben van Boxtel Johan H. van Es Johan Offerhaus Peter J. Peters Jacco van Rheenen Michiel Vermeulen Hans Clevers 《Cell Stem Cell》2019,24(6):927-943.e6
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