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PMID:20478417
| Citation |
Suzuki, H, Yamada, S, Toyama, Y and Takeda, S (2010) The C-terminal domain is sufficient for host-binding activity of the Mu phage tail-spike protein. Biochim. Biophys. Acta 1804:1738-42 |
|---|---|
| Abstract |
The Mu phage virion contains tail-spike proteins beneath the baseplate, which it uses to adsorb to the outer membrane of Escherichia coli during the infection process. The tail spikes are composed of gene product 45 (gp45), which contains 197 amino acid residues. In this study, we purified and characterized both the full-length and the C-terminal domains of recombinant gp45 to identify the functional and structural domains. Limited proteolysis resulted in a Ser64-Gln197 sequence, which was composed of a stable C-terminal domain. Analytical ultracentrifugation of the recombinant C-terminal domain (gp45-C) indicated that the molecular weight of gp45-C was about 58 kDa and formed a trimeric protomer in solution. Coprecipitation experiments and a quartz crystal microbalance (QCM) demonstrated that gp45-C irreversibly binds to the E. coli membrane. These results indicate that gp45 shows behaviors similar to tail-spike proteins of other phages; however, gp45 did not show significant sequence homology with the other phage tail-spike structures that have been identified. |
| Links |
PubMed Online version:10.1016/j.bbapap.2010.05.003 |
| Keywords |
Bacteriophage mu/growth & development; Bacteriophage mu/metabolism; Escherichia coli/genetics; Escherichia coli/metabolism; Protein Structure, Tertiary; Recombinant Proteins/genetics; Recombinant Proteins/isolation & purification; Recombinant Proteins/metabolism; Viral Tail Proteins/genetics; Viral Tail Proteins/isolation & purification; Viral Tail Proteins/metabolism |
| edit table |
Significance
Annotations
| Gene product | Qualifier | GO Term | Evidence Code | with/from | Aspect | Extension | Notes | Status |
|---|---|---|---|---|---|---|---|---|
| GO:0046812: host cell surface binding |
ECO:0000314: |
F |
Figures 4A and 5 show GP45 and GP45C binding to E. coli cell membranes. |
complete | ||||
Notes
See also
References
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