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.