Molecular characterization of an ice nucleation protein variant (InaQ) from Pseudomonas syringae and the analysis of its transmembrane transport activity in Escherichia coli

International Journal of Biological Sciences

Volumn 8, Issue 8, 2012, Pages 1097-1108

  Li, Qianqian ^a   Yan, Qi ^a   Chen, Jinsi ^a   He, Yan ^a   Wang, Jing ^a   Zhang, Hongxing ^a   Yu, Ziniu ^a   Li, Lin ^a  

^a HUAZHONG AGRICULTURAL UNIVERSITY   (China)

Author keywords

Escherichia coli; Expression; Ice nucleation protein; Pseudomonas syringae; Transport

Indexed keywords

GREEN FLUORESCENT PROTEIN; ICE NUCLEATION PROTEIN; OUTER MEMBRANE PROTEIN; PRIMER DNA;

AMINO ACID SEQUENCE; ARTICLE; CHEMICAL PHENOMENA; CHEMICAL STRUCTURE; CHEMISTRY; DNA SEQUENCE; ESCHERICHIA COLI; FLOW CYTOMETRY; FLUORESCENCE; FLUORESCENCE MICROSCOPY; GENETICS; METABOLISM; MOLECULAR CLONING; MOLECULAR GENETICS; NUCLEOTIDE SEQUENCE; PHYSIOLOGY; PLASMID; PSEUDOMONAS SYRINGAE; TRANSPORT AT THE CELLULAR LEVEL; WESTERN BLOTTING;

AMINO ACID SEQUENCE; BACTERIAL OUTER MEMBRANE PROTEINS; BASE SEQUENCE; BIOLOGICAL TRANSPORT; BLOTTING, WESTERN; CLONING, MOLECULAR; DNA PRIMERS; ESCHERICHIA COLI; FLOW CYTOMETRY; FLUORESCENCE; GREEN FLUORESCENT PROTEINS; HYDROPHOBIC AND HYDROPHILIC INTERACTIONS; MICROSCOPY, FLUORESCENCE; MODELS, MOLECULAR; MOLECULAR SEQUENCE DATA; PLASMIDS; PSEUDOMONAS SYRINGAE; SEQUENCE ANALYSIS, DNA;

EID: 84867556035     PISSN: 14492288     EISSN: None     Source Type: Journal    
DOI: 10.7150/ijbs.4524     Document Type: Article

References (26)

1. Bender C, Alarcon-Chaidez F, Gross D. Pseudomonas syringae phytotoxins: mode of action, regulation, and biosynthesis by peptide and polyketide synthetases. Microbiol Mol Biol Rev. 1999; 63: 266-92.
2. Collmer A, Badel JL, Charkowski AO, et al. Pseudomonas syringae Hrp type III secretion system and effector proteins. Proc Natl Acad Sci USA. 2000; 97: 8770-7.
3. Hirano SS, Upper CD. Bacteria in the leaf ecosystem with emphasis on Pseudomonas syringae-a pathogen, ice nucleus, and epiphyte. Microbiol Mol Biol Rev. 2000; 64: 624-53.
4. Cochet N, Widehem P. Ice crystallization by Pseudomonas syringae. Appl Microbiol Biotechnol. 2000; 54: 153-61.
5. Gurian-Sherman D, Lindow SE. Bacterial ice nucleation: significance and molecular basis. FASEB J. 1993; 7: 1338-43.
6. Lee SY, Choi JH, Xu Z. Microbial cell-surface display. Trends Biotechnol. 2003; 21: 45-52.
7. Daugherty PS. Protein engineering with bacterial display. Curr Opin Struct Biol. 2007; 17: 474-80.
8. Kawahara H. The structures and functions of ice crystal-controlling proteins from bacteria. J Biosci Bioeng. 2002; 94: 492-6.
9. Jung HC, Lebeault JM, Pan JG. Surface display of Zymomonas mobilis levansucrase by using the ice-nucleation protein of Pseudomonas syringae. Nat Biotechnol. 1998; 16: 576-80.
10. Schmid D, Pridmore D, Capitani G, et al. Molecular organisation of the ice nucleation protein InaV from Pseudomonas syringae. FEBS Lett. 1997; 414: 590-4.
11. Green RL, Warren GJ. Physical and functional repetition in a bacterial ice nucleation gene. Nature. 1985; 317: 645-8.
12. Turner MA, Arellano F, Kozloff LM. Components of ice nucleation structures of bacteria. J Bacteriol. 1991; 173: 6515-27.
13. Kozloff LM, Turner MA, Arellano F, et al. Phosphatidylinositol, a phospholipid of ice-nucleating bacteria. J Bacteriol. 1991; 173: 2053-60.
14. Ferguson MA, Williams AF. Cell-surface anchoring of proteins via glycosyl-phosphatidylinositol structures. Annu Rev Biochem. 1988; 57: 285-320.
15. Li L, Kang DG, Cha HJ. Functional display of foreign protein on surface of Escherichia coli using N-terminal domain of ice nucleation protein. Biotechnol Bioeng. 2004; 85: 214-21.
16. Li Q, Yu Z, Shao X, et al. Improved phosphate biosorption by bacterial surface display of phosphate-binding protein utilizing ice nucleation protein. FEMS Microbiol Lett. 2009; 299: 44-52.
17. Wu ML, Tsai CY, Chen TH. Cell surface display of Chi92 on Escherichia coli using ice nucleation protein for improved catalytic and antifungal activity. FEMS Microbiol Lett. 2006; 256: 119-25.
18. Lee JS, Shin KS, Pan JG, et al. Surface-displayed viral antigens on Salmonella carrier vaccine. Nat Biotechnol. 2000; 18: 645-8.
19. Xu Y, Liu Q, Zhou L, et al. Surface display of GFP by Pseudomonas syringae truncated ice nucleation protein in attenuated Vibrio anguillarum strain. Mar Biotechnol (NY). 2008; 10: 701-8.
20. Shimazu M, Nguyen A, Mulchandani A, et al. Cell surface display of organophosphorus hydrolase in Pseudomonas putida using an ice-nucleation protein anchor. Biotechnol Prog. 2003; 19: 1612-4.
21. Chungjatupornchai W, Fa-aroonsawat S. Translocation of green fluorescent protein to cyanobacterial periplasm using ice nucleation protein. J Microbiol. 2009; 47: 187-92.
22. Jung HC, Park JH, Park SH, et al. Expression of carboxymethylcellulase on the surface of Escherichia coli using Pseudomonas syringae ice nucleation protein. Enzyme Microb Technol. 1998; 22: 348-54.
23. Li Q, Ni H, Meng S, et al. Suppressing Erwinia carotovora pathogenicity by projecting N-acyl homoserine lactonase onto the surface of Pseudomonas putida cells. J Microbiol Biotechnol. 2011; 21: 1330-5.
24. Sambrook J, Russell DW. Molecular cloning: a laboratory manual, 3rd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory Press. 2001.
25. Nielsen H, Engelbrecht J, Brunak S, et al. Identification of prokaryotic and eukaryotic signal peptides and prediction of their cleavage sites. Protein Eng. 1997; 10: 1-6.
26. Shi H, Wen SW. Display of green fluorescent protein on Escherichia coli cell surface. Enzyme Microb Technol. 2001; 28: 25-34.