Difference between revisions of "Part:BBa K1894000"
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<partinfo>BBa_K1894000 short</partinfo> | <partinfo>BBa_K1894000 short</partinfo> | ||
− | The gene GvpA1 can express GvpA protein, which acts as the main structural protein of gas vesicle in Microcystis aeruginosa. | + | The gene GvpA1 can express GvpA protein, which acts as the main structural protein of gas vesicle in Microcystis aeruginosa. We mutate GvpA1 gene in order to limit the level of GvpA1 expression and change the conformation of gas vesicle protein---- a possible strategy to disrupt the distribution of microcysis in water and control algae bloom.By changing two base pairs, we mutate a serine to an alanine (hydrophilic amino acid to hydrophobic amino acid) and an alanine to a glycin. |
− | |||
===Usage and Biology=== | ===Usage and Biology=== | ||
+ | Gas vesicle protein, which widely exists in all forms of planktonic cyanobacteria, provides cells with buoyancy by changing the density of cells and regulates their vertical distributions in natural waters, enabling them to achieve ideal vertical position in water for growth and subsequent niche colonization. | ||
+ | GvpA protein forms the skeleton of gas vesicle and acts as the main structural protein. Therefore, we plans to mutate GvpA1 gene in order to limit the level of GvpA1 expression and change the conformation of gas vesicle protein---- a possible strategy to disrupt the distribution of microcysis in water and control algae bloom. By changing two base pairs, we mutate a serine to an alanine (hydrophilic amino acid to hydrophobic amino acid) and an alanine to a glycin. | ||
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Revision as of 02:09, 20 October 2016
Modified GvpA1 coding region
The gene GvpA1 can express GvpA protein, which acts as the main structural protein of gas vesicle in Microcystis aeruginosa. We mutate GvpA1 gene in order to limit the level of GvpA1 expression and change the conformation of gas vesicle protein---- a possible strategy to disrupt the distribution of microcysis in water and control algae bloom.By changing two base pairs, we mutate a serine to an alanine (hydrophilic amino acid to hydrophobic amino acid) and an alanine to a glycin.
Usage and Biology
Gas vesicle protein, which widely exists in all forms of planktonic cyanobacteria, provides cells with buoyancy by changing the density of cells and regulates their vertical distributions in natural waters, enabling them to achieve ideal vertical position in water for growth and subsequent niche colonization. GvpA protein forms the skeleton of gas vesicle and acts as the main structural protein. Therefore, we plans to mutate GvpA1 gene in order to limit the level of GvpA1 expression and change the conformation of gas vesicle protein---- a possible strategy to disrupt the distribution of microcysis in water and control algae bloom. By changing two base pairs, we mutate a serine to an alanine (hydrophilic amino acid to hydrophobic amino acid) and an alanine to a glycin.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]