Deciphering the unique cellulose degradation mechanism of the ruminal bacterium Fibrobacter succinogenes S85.
Sci Rep
; 9(1): 16542, 2019 11 12.
Article
in En
| MEDLINE
| ID: mdl-31719545
ABSTRACT
Fibrobacter succinogenes S85, isolated from the rumen of herbivores, is capable of robust lignocellulose degradation. However, the mechanism by which it achieves this is not fully elucidated. In this study, we have undertaken the most comprehensive quantitative proteomic analysis, to date, of the changes in the cell envelope protein profile of F. succinogenes S85 in response to growth on cellulose. Our results indicate that the cell envelope proteome undergoes extensive rearrangements to accommodate the cellulolytic degradation machinery, as well as associated proteins involved in adhesion to cellulose and transport and metabolism of cellulolytic products. Molecular features of the lignocellulolytic enzymes suggest that the Type IX secretion system is involved in the translocation of these enzymes to the cell envelope. Finally, we demonstrate, for the first time, that cyclic-di-GMP may play a role in mediating catabolite repression, thereby facilitating the expression of proteins involved in the adhesion to lignocellulose and subsequent lignocellulose degradation and utilisation. Understanding the fundamental aspects of lignocellulose degradation in F. succinogenes will aid the development of advanced lignocellulosic biofuels.
Full text:
1
Collection:
01-internacional
Database:
MEDLINE
Main subject:
Rumen
/
Cellulose
/
Fibrobacter
Limits:
Animals
Language:
En
Journal:
Sci Rep
Year:
2019
Document type:
Article
Affiliation country:
United kingdom