Difference between revisions of "Part:BBa K5477007"
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In our system, pPOP6 is used to drive the expression of our receptor modules - LexA domain fused with ligand-binding domain of Estrogen Receptor alpha <b>LexA-ERα</b> and with Estrogen-related Receptor gamma ligand-binding domain <b>LexA-ERRγ</b>.
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In our system, pPOP6 is used to drive the expression of our receptor modules - LexA domain fused with ligand-binding domain of Estrogen Receptor alpha <b>LexA-ERα</b> [https://parts.igem.org/Part:BBa_K5477028 | BBa_K5477028] .  
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Revision as of 14:10, 29 September 2024


pPOP6 - weak constitutive promoter in Saccharomyces cerevisiae

POP6 encodes a subunit of RNase MRP, nuclear RNase P, and telomerase, which are involved in key RNA processing functions. RNase MRP cleaves pre-rRNA, while nuclear RNase P processes tRNA precursors and facilitates RNA turnover. Telomerase, in which POP6 plays a role, replenishes telomeric DNA. POP6 forms a heterodimer with Pop7p, binding the P3 domain of RNase MRP and RNase P RNAs (1) (2) (3) (4).


From a paper of Lee et al. 2015, Figure 3A shows the relative strengths of 19 constitutive promoters by measuring fluorescence from two reporters, mRuby2 and Venus.

promoters.gif

The plot highlights three key promoters: pTDH3 (strong), pRPL18B (medium), and pREV1 (weak) (2). The horizontal and vertical bars represent the range of fluorescence from four biological replicates, with the intersection indicating the median. The inset also includes results from testing a third reporter, mTurquoise2, demonstrating consistent promoter strength across different reporter proteins. From the data, pPOP6 appears to be positioned in the lower range of constitutive promoter strengths.


In our system, pPOP6 is used to drive the expression of our receptor modules - LexA domain fused with ligand-binding domain of Estrogen Receptor alpha LexA-ERα | BBa_K5477028 .

Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BamHI site found at 73
    Illegal BamHI site found at 390
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]



References

1. Chamberlain JR, Lee Y, Lane WS, Engelke DR. Purification and characterization of the nuclear RNase P holoenzyme complex reveals extensive subunit overlap with RNase MRP. Genes Dev. 1998 Jun 1;12(11):1678-90. doi: 10.1101/gad.12.11.1678. PMID: 9620854; PMCID: PMC316871.

2. Houser-Scott F, Xiao S, Millikin CE, Zengel JM, Lindahl L, Engelke DR. Interactions among the protein and RNA subunits of Saccharomyces cerevisiae nuclear RNase P. Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2684-9. doi: 10.1073/pnas.052586299. PMID: 11880623; PMCID: PMC122408.

3. Lee, Michael & DeLoache, William & Cervantes, Bernardo & Dueber, John. (2015). A Highly Characterized Yeast Toolkit for Modular, Multipart Assembly. ACS synthetic biology. 4. 10.1021/sb500366v.

4. Perederina A, Esakova O, Koc H, Schmitt ME, Krasilnikov AS. Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs. RNA. 2007 Oct;13(10):1648-55. doi: 10.1261/rna.654407. Epub 2007 Aug 23. PMID: 17717080; PMCID: PMC1986809.