Difference between revisions of "Part:BBa K2378007"

Revision as of 20:58, 1 November 2017

IrrE Coding Sequence

This is improved coding sequence of IrrE from BBa_K729001 (https://parts.igem.org/Part:BBa_K729001) by Team UCL London 2012. When transformed to E. coli, this protein protected from salt, oxidative, and thermal shock.

Background of Improvement

We tried to analyse existing IrrE part from BBa_K729001 Team UCL London, and found some possible error in the coding sequence. The translated nucleotide is not a contiguous protein, which is shown by a stop codon in the middle of the coding sequence, continued by another start codon ~90 base downstream.

At first, we thought that it's the IrrE nature to have two separate active proteins. But after we find the corresponding Uniprot accession number, there are important domain of protein in the 75-199 position of the residues, under the classification of peptidases. This domain is essential for the activity of IrrE functionality because it cleaves and inactivates repressor protein DdrO, leading to the upregulation of several DNA repair and other genes after exposure of the cells to radiation.^{<a href="https://www.ncbi.nlm.nih.gov/pubmed/25170972"> 1 </a>}

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
INCOMPATIBLE WITH RFC[25]
Illegal AgeI site found at 489
Illegal AgeI site found at 606
1000
COMPATIBLE WITH RFC[1000]

@@ Line 9: / Line 9: @@
 We tried to analyse existing IrrE part from BBa_K729001 Team UCL London, and found some possible error in the coding sequence. The translated nucleotide is not a contiguous protein, which is shown by a stop codon in the middle of the coding sequence, continued by another start codon ~90 base downstream.
-At first, we thought that it's the IrrE nature to have two separate active proteins. But after we find the corresponding Uniprot accession number, there are important domain of protein in the 75-199 position of the residues, under the classification of peptidases. This domain is essential for the activity of IrrE functionality because it cleaves and inactivates repressor protein DdrO, leading to the upregulation of several DNA repair and other genes after exposure of the cells to radiation.<sup>[<a href="https://www.ncbi.nlm.nih.gov/pubmed/25170972">1</a> ]</sup>
+At first, we thought that it's the IrrE nature to have two separate active proteins. But after we find the corresponding Uniprot accession number, there are important domain of protein in the 75-199 position of the residues, under the classification of peptidases. This domain is essential for the activity of IrrE functionality because it cleaves and inactivates repressor protein DdrO, leading to the upregulation of several DNA repair and other genes after exposure of the cells to radiation.<sup><a href="https://www.ncbi.nlm.nih.gov/pubmed/25170972"> 1 </a></sup>
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