Difference between revisions of "Part:BBa K2959009"

 
 
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<partinfo>BBa_K2959009 short</partinfo>
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<partinfo>BBa_K2959009 short</partinfo><br>
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AtPFN1 is a protein extracted from the plant Arabidopsis thaliana. It is a profilin which means that is an actin binding protein. AtPFN1 inhibits fungal growth  by penetrating the cell wall and membrane, generating reactive oxygen species and mitochondrial superoxide triggering cell apoptosis, resulting in morphological changes in the cells1.
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AtPFN1 is a protein extracted from the plant <i>Arabidopsis thaliana</i>. It is a profilin which means that is an actin binding protein. AtPFN1 inhibits fungal growth  by penetrating the cell wall and membrane, generating reactive oxygen species and mitochondrial superoxide triggering cell apoptosis, resulting in morphological changes in the cells<sup>1</sup>.
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The binding affinity of antifungal proteins to fungal cells is the most important attribute for their fungal action, even if the mechanism is membranolytic or cell damaging. It has also been demonstrated that these proteins can be transferred across the cell membrane into the cytosolic space and accumulate in the cytosol of the cell by altering the membrane integrity. For cytosolic translocation the mechanisms used by the proteins are direct penetration, vacuolar localization and expansion, partial plasma membrane disruption, transition pore formation and endocytosis. AtPFN1 has exhibited a potent antifungal activity against fungal strains of C. gloesporioides, F. osysporum, C. albicans, and C. glabrata1.
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The binding affinity of antifungal proteins to fungal cells is the most important attribute for their fungal action, even if the mechanism is membranolytic or cell damaging. It has also been demonstrated that these proteins can be transferred across the cell membrane into the cytosolic space and accumulate in the cytosol of the cell by altering the membrane integrity. For cytosolic translocation the mechanisms used by the proteins are direct penetration, vacuolar localization and expansion, partial plasma membrane disruption, transition pore formation and endocytosis. AtPFN1 has exhibited a potent antifungal activity against fungal strains of <i>C. gloesporioides</i>, <i>F. osysporum</i>, <i>C. albicans</i>, and <i>C. glabrata</i><sup>1</sup>.
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<span class='h3bb'>Sequence and Features</span>
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===Sequence and Features===
 
<partinfo>BBa_K2959009 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2959009 SequenceAndFeatures</partinfo>
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===References===
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1. Park, S. C., Kim, I. R., Kim, J. Y., Lee, Y., Kim, E. J., Jung, J. H., ... & Lee, J. R. (2018). Molecular mechanism of Arabidopsis thaliana profilins as antifungal proteins. Biochimica et Biophysica Acta (BBA)-General Subjects, 1862(12), 2545-2554. doi:10.1016/j.bbagen.2018.07.028
  
  

Latest revision as of 22:10, 19 October 2019


Arabidopsis thaliana Profilin 1

AtPFN1 is a protein extracted from the plant Arabidopsis thaliana. It is a profilin which means that is an actin binding protein. AtPFN1 inhibits fungal growth by penetrating the cell wall and membrane, generating reactive oxygen species and mitochondrial superoxide triggering cell apoptosis, resulting in morphological changes in the cells1.
The binding affinity of antifungal proteins to fungal cells is the most important attribute for their fungal action, even if the mechanism is membranolytic or cell damaging. It has also been demonstrated that these proteins can be transferred across the cell membrane into the cytosolic space and accumulate in the cytosol of the cell by altering the membrane integrity. For cytosolic translocation the mechanisms used by the proteins are direct penetration, vacuolar localization and expansion, partial plasma membrane disruption, transition pore formation and endocytosis. AtPFN1 has exhibited a potent antifungal activity against fungal strains of C. gloesporioides, F. osysporum, C. albicans, and C. glabrata1.

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]

References

1. Park, S. C., Kim, I. R., Kim, J. Y., Lee, Y., Kim, E. J., Jung, J. H., ... & Lee, J. R. (2018). Molecular mechanism of Arabidopsis thaliana profilins as antifungal proteins. Biochimica et Biophysica Acta (BBA)-General Subjects, 1862(12), 2545-2554. doi:10.1016/j.bbagen.2018.07.028