Difference between revisions of "Part:BBa K5317014"

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===Theoretical Part Design===
 
===Theoretical Part Design===
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This part was codon optimised for human cell lines.
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This part was codon optimised for human cell lines. This part was amplified by using the primers in table 1.
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      <title>HTML Table Caption</title>
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<caption>Table1: Primers used to extract the ccpA gene sequence.</caption>
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<table style="width:70%">
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    <th>Primer name</th>
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    <th>Sequence</th>
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    <td>ccpA_fw_1</td>
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    <td>tggatccccttttgtagttcctcggtattcaattctgtgag</td>
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    <td>ccpA_rv</td>
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    <td>TGAACCGTCAGATCCGatgacagttactatatatgatgtagcaagagaagc</td>
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</table>
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</body>
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===Sequence and Features===
 
===Sequence and Features===

Revision as of 15:52, 26 September 2024


CcpA

Usage and Biology

The regulatory functions of CcpA are modulated by phosphorylation by serine/threonine kinases, which can affect its DNA-binding activity and thus its ability to regulate target genes. This phosphorylation-dependent mechanism enables S. aureus to adapt to different environmental conditions, thereby increasing its survivability and virulence (Liao et al., 2022). We used this bacterial protein to evaluate the interaction with the PknB kinase.

Cloning

Theoretical Part Design

This part was codon optimised for human cell lines. This part was amplified by using the primers in table 1.

HTML Table Caption Table1: Primers used to extract the ccpA gene sequence.

Primer name Sequence
ccpA_fw_1 tggatccccttttgtagttcctcggtattcaattctgtgag
ccpA_rv TGAACCGTCAGATCCGatgacagttactatatatgatgtagcaagagaagc


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

Liao, X., Li, H., Guo, Y., Yang, F., Chen, Y., He, X., Li, H., Xia, W., Mao, Z.-W., & Sun, H. (2022). Regulation of DNA-binding activity of the Staphylococcus aureus catabolite control protein A by copper (II)-mediated oxidation. Journal of Biological Chemistry, 298(3), 101587. https://doi.org/10.1016/j.jbc.2022.101587