Reporter

Part:BBa_K763001

Designed by: Pedro Luis Dorado Morales   Group: iGEM12_Valencia_Biocampus   (2012-09-07)
Revision as of 09:33, 7 September 2012 by Registry (Talk | contribs)

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pGroE + Gene encoding AsRed2

When the bacteria suffer heat shock the protein gets expressed. Why?

Heat-shock response is mediated by the Sigma 32 factor. This alternative sigma factor lets the RNA polymerase binds to some consensus promoter sequence.

groE has this sequence in the promoter. That is because this gene encodes a chaperon protein, GroE. Chaperone proteins are a group of proteins present in all cells, many of them are heat shock proteins, whose function is to assist the folding of other proteins in the newly formed protein synthesis.

In the case of GroE, it processes a nonnative polypeptide in a cycle consisting of three steps. First, the polypeptide substrate is captured by GroEL. Upon binding of the co-chaperone GroES and ATP, the substrate is then discharged into a unique microenvironment inside of the chaperone, which promotes proper folding. After hydrolysis of ATP, the polypeptide is released into solution. Moreover, GroE may actively increase the folding efficiency, e.g. by unfolding of misfolded protein molecules. This chaperon has an important role in heat shock proccess too, helping other proteins not to denature.


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 NgoMIV site found at 507
  • 1000
    COMPATIBLE WITH RFC[1000]


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