A genetically engineered protein domain binding to bacterial murein, archaeal pseudomurein, and fungal chitin cell wall materialVisweswaran, G. R. R., Dijkstra, B. W. & Kok, J., Nov-2012, In : Applied Microbiology and Biotechnology. 96, 3, p. 729-737 9 p.
Research output: Contribution to journal › Article › Academic › peer-review
The major murein and pseudomurein cell wall-binding domains, i.e., the Lysin Motif (LysM) (Pfam PF01476) and pseudomurein cell wall-binding (PMB) (Pfam PF09373) motif, respectively, were genetically fused. The fusion protein is capable of binding to both murein- and pseudomurein-containing cell walls. In addition, it also binds to chitin, the major polymer of fungal cell walls. Binding is influenced by pH and occurs at a pH close to the pI of the binding protein. Functional studies on truncated versions of the fusion protein revealed that murein and chitin binding is provided by the LysM domain, while binding to pseudomurein is achieved through the PMB domain.
|Number of pages||9|
|Journal||Applied Microbiology and Biotechnology|
|Publication status||Published - Nov-2012|
- Murein, Pseudomurein, Chitin, Domain, SURFACE DISPLAY SYSTEM, LACTIC-ACID BACTERIA, LACTOCOCCUS-LACTIS, LYSM DOMAINS, PEPTIDOGLYCAN HYDROLASE, METHANOBACTERIUM-THERMOAUTOTROPHICUM, HETEROLOGOUS PROTEINS, ESCHERICHIA-COLI, GEM PARTICLES, LYTIC ENZYME