Part:BBa_K2273034
| Part Information | |
|---|---|
| BioBrick Nr. | BBa_K2273034 |
| RFC standard | RFC 25 |
| Requirement | pSB1C3 |
| Original Biobrick Part | BBa_J06504: mCherry |
| Submitted by | [http://2017.igem.org/Team:TU_Dresden TU Dresden] |
Codon-optimized mCherry for Bacillus subtilis
Brief introduction in Fluorescent Proteins
Fluorescent proteins are small proteins with β-barrel-fold topology. They are useful for tracking global expression of target genes and localizations of these genes inside/outside cells. The unique chromophore in each fluorescent protein, originates from three intrinsic amino acids, at positions 65â67. The chromophore is tightly enclosed inside the protein and its formation does not require any cofactors or enzymes but only molecular oxygen. The rigidity of the β-barrel protects the chromophore from the environment and from radiationless decay. It also restricts chromophore flexibility as the correct folding of the protein is required for the chromophore formation. Proper orientation of the amino acids is necessary for chromophore maturation as it catalyzes chromophore synthesis.
Overview of mCherry
mCherry is a red fluorescent protein that has an excitation peak 585 nm and a peak emission at 615 nm. It originates from a protein isolated Discosoma sp., which a mushroom coral, and is very stable and resistant to photobleaching. It matures very quickly after transcription, making detection very quick.
mCherry expression in Bacillus subtilis
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]
| None |