Composite

Part:BBa_K1365006

Designed by: Sandra Mous   Group: iGEM14_Groningen   (2014-09-24)
Revision as of 13:48, 20 October 2021 by Shubhmay 8380 (Talk | contribs)

NisR and NisK

Usage and Biology

This BioBrick contains the coding parts for the genes NisR and NisK. NisK is a membrane-associated protein kinase that phosphorylates NisR in response to nisin in the environment. NisR is a regulatory protein, regulating promoters like PNisA and PNisI.

Together with the genes NisA, NisB, NisC, NisP they are responsible for producing the lantibiotic nisin in Lactococcus lactis, see the figure below. The NisA protein is first modified and then transported out of the cell. The serines and threonines of NisA are dehydrated by NisB and then the precursor is cyclized by NisC. After this process, the precursor is transported out of the cell (2). Here, the lead peptide is cut off by NisP (3) and the mature nisin is formed.1

Nisin casette.art.png

Nisin is a lantibiotic, an bacteriocidal peptide. Nisin inhibits the growth of a broad range of Gram positive bacteria, of which many are spoilage bacteria or pathogens. Nisin is therefore extensively used in the food industry as a preservative. Nisin forms pores in the membrane of the bacteria it kills and inhibits the peptidoglycan synthesis.2


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. Cheigh, C. I. and Pyun, Y.R. (2005) Nisin biosynthesis and its properties. Biotechnol. Lett. 27: 1641-1648
2. Zhou, H. et al. (2014) Mechanisms of nisin resistance in Gram-positive bacteria. Ann. Microbiol. 64: 413-420

Contribution by Team IISER_Kolkata 2021

Group: iGEM21_IISER_Kolkata
Author: Soumi Bhattacharyya, Shubhamay Das
Summary: We learnt that Team iGEM17_Munich has performed the assay for target-dependent activity of purified Cas13a protein under different concentrations of target RNA molecules. Team ZJUT_China_B 2020 has characterized the base preference of collateral cleavage activity of LwaCas13a protein. Due to limitations in laboratory access, we have contributed more information about this part through literature survey.

New information:


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