Part:BBa_K265008:Design
Ice Nucleation Protein NC
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 405
- 1000COMPATIBLE WITH RFC[1000]
Design Notes
INPNC was put in RFC12 format to accommodate fusion proteins. INPNC is anchored to the cell surface by a glycosyl-phosphatidylinositol (GPI) anchor. The full length ice-nucleation protein is made of 3 parts--the N-terminal, the C-terminal, and a central domain. In this truncated version (INPNC), just the N-terminal and C-terminal domains are included, indicated by the 'NC' in INPNC. Both the full and truncated versions of INP will display fused proteins on the cell surface although transporting the protein across the inner membrane may be improved with the addition of a proteolytic cleavage sequence such as BBa_K265002.
Source
Synthesized from Mr. Gene. Gene originates from Pseudomonas syringae
References
1. Edwin van Bloois. Remko T. Winter. Dick B. Janssen, Marco W. Fraaije. 2009, Export of functional Streptomyces coelicolor alditol oxidase to the periplasm or cell surface of Escherichia coli and its application in whole-cell biocatalysis. (2009). Appl. Microbiol. Biotechnol. 83. p. 679-687.
2. Se Whan Park, Moon Gyu Chung, Hwa Young Lee, Jeong Yoon Kim, and Young Ha Rhee. (2008). Stable expression and secretion of the polyhydroxybutyrate depolymerase of Paucimonas lemoignei in Escherichia coli. J. Microbiology. 46(6). pp. 662-669.
3. Heung-Chae Junge, Joon-Hyun Park, Seung-Hwan Park, Jean-Michel Lebeault, and Jae-Gu Pan. (1998). Expression of carboxymethylcellulase on the Surface of Escerichia coli using Pseudomonas syringae ice nucleation protein. Enzyme and Microbial Technology. 22: 348-354, 1998.