10.6084/m9.figshare.c.3778634_D4.v1 Jie Zhang Jie Zhang Shiyue Liu Shiyue Liu Renmin Li Renmin Li Wei Hong Wei Hong Yan Xiao Yan Xiao Yingang Feng Yingang Feng Qiu Cui Qiu Cui Ya-Jun Liu Ya-Jun Liu MOESM3 of Efficient whole-cell-catalyzing cellulose saccharification using engineered Clostridium thermocellum Springer Nature 2017 β-Glucosidase Cellulosome CelS Fermentable sugar Genome editing Lignocellulose 2017-05-12 05:00:00 Figure https://springernature.figshare.com/articles/figure/MOESM3_of_Efficient_whole-cell-catalyzing_cellulose_saccharification_using_engineered_Clostridium_thermocellum/5004623 Additional file 3: Figure S3. Identification of fusion protein Cel-BGL-Doc peptides in the parent and ΔpyrF::CaBglA strains by mass spectroscopy analysis. Cellulosomal and extracellular proteins with the size of ~135 kDa or ~75 kDa were investigated. The green highlights indicate peptides detected by mass spectroscopy. The amino acid sequences shown in black, purple, and blue belong to Cel (the catalyzing module of CelS), BGL (CaBglA), and Doc (the assembling module of CelS), respectively. The linker sequences are shown in bold. The insertion sites of the BGL sequence are indicated by red triangles. CaBglA sequences are detected in ~135-kDa but not ~75-kDa cellulosomal and extracellular proteins of ∆pyrF::CaBglA, indicating the successful expression, secretion, and cellulosomal assembly of the protein Cel-CaBglA-Doc in ΔpyrF::CaBglA.