Team:Cambridge/BioBricks
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The Cambridge iGEM team has submitted 20 parts to the [http://partsregistry.org/Main_Page Registry of Standard Biological Parts]. Many of these parts have been extensively characterised. This data is stored in the Parts Registry, you can click on any BioBrick to view its technical datasheet. | The Cambridge iGEM team has submitted 20 parts to the [http://partsregistry.org/Main_Page Registry of Standard Biological Parts]. Many of these parts have been extensively characterised. This data is stored in the Parts Registry, you can click on any BioBrick to view its technical datasheet. | ||
=Featured parts= | =Featured parts= |
Revision as of 12:35, 27 October 2010
Parts submitted
The Cambridge iGEM team has submitted 20 parts to the [http://partsregistry.org/Main_Page Registry of Standard Biological Parts]. Many of these parts have been extensively characterised. This data is stored in the Parts Registry, you can click on any BioBrick to view its technical datasheet.
Featured parts
BBa_K325219 |
Red luciferase and LRE operon from L. cruciata under pBADThis part generates the luciferase and luciferin regenerating enzyme proteins from the Japanese firefly, Luciola cruciata, when induced by L-arabinose. The luciferase produced has a point mutation Ser286Asn which gives it a redshifted emission spectrum as compared to wild-type. The sequence of nucleotides is codon optimised for expression in E. coli. |
BBa_K325909 |
V. fischeri luxCDABE under pBADThis part generates luxCDABE proteins from the bioluminescent bacterium, Vibrio fischeri, when induced by L-arabinose. The BioBrick produces light from basic metabolites found in E. coli, luxCDE produce the substrate used by luxAB for bioluminescence. The part creates a blue light. |
Parts based on bacterial systems
BBa_K325902 |
V. fischeri luxCDThis is a translational unit designed to produce V. fischeri luxC and luxD genes when placed under a suitable promoter. The DNA sequence is codon optimised for expression in E. coli. Both proteins are part of the fatty aldehyde synthesis pathway. luxC is a reductase and luxD is a acyltransferase. LuxE must also be supplied to complete the pathway for fatty aldehyde synthesis. Such fatty aldehydes are the substrate for the luxAB bacterial luciferase. |
BBa_K325903 |
V. fischeri luxEGThis is a translational unit designed to produce V. fischeri luxE and luxG genes when placed under a suitable promoter. The DNA sequence is codon optimised for expression in E. coli. luxE functions as the synthetase creating fatty aldehydes for bioluminescence. LuxG is a flavin reductase. |
BBa_K325905 |
luxCDEG pLambda ABThis part constitutively expresses [http://partsregistry.org/wiki/index.php?title=Part:BBa_K216008 the Xenorhabdus luminescens luxAB luciferase] already in the registry. It also features a translational unit for the substrate generating luxCDEG from Vibrio fischeri. This means that only when supplied with PoPs will it produce light output. |
BBa_K325906 |
pBAD luxCDEG pLambda ABThis is the same as the part above but was built for testing induction by adding the pBAD promoter, making light inducible by addition of L-arabinose. |
Firefly luciferases
BBa_K325101 |
Luciferase from Photinus pyralis with increased substrate affinityThis is a translational unit for a mutated and codon-optimised form of the luciferase from the North American firefly, Photinus pyralis. It is described in [http://www.ncbi.nlm.nih.gov/pubmed/17540326 Fujii et al. 2007] as having a 10 times higher substrate affinity and luminescence output compared to wildtype. |
BBa_K325108 |
P.pyralis luciferase under pBADThis is the same as the part above but placed under the pBAD promoter induced by L-arabinose for characterisation. |
BBa_K325211 |
L. cruciata luciferase (red mutant)This is a translational unit for a mutant (Ser286Asn) and codon-optimised luciferase from the Japanese firefly, Luciola cruciata. It is deeply red-shifted as compared to wild type. |
BBa_K325218 |
L. cruciata luciferase under pBADThis is the same as the part above but placed under the pBAD promoter induced by L-arabinose for characterisation. |
Firefly luciferin regenerating enzymes
BBa_K325102 |
P. pyralis Luciferin Regenerating EnzymeThis is a translational unit for a codon-optimised Luciferin Regenerating Enzyme (LRE) from the North American firefly, Photinus pyralis. |
BBa_K325202 |
L. cruciata Luciferin Regenerating EnzymeThis is a translational unit for a codon-optimised Luciferin Regenerating Enzyme (LRE) from the Japanese firefly, Luciola cruciata. |
Firefly luciferase, LRE operons
BBa_K325210 |
Luciola cruciata LRE and luciferaseThis translational unit combines the luciferin regenerating enzyme (BBa_K325202) and red-shifted luciferase (BBa_K325211) from the Japanese firefly, Luciola cruciata. The luciferin regenerating enzyme helps to strengthen and sustain light output. |
BBa_K325100 |
Photinus pyralis LRE and luciferaseThis part combines the luciferin regenerating enzyme (BBa_K325102) and luciferase (BBa_K325101) from the North American firefly, Photinus pyralis. The luciferin regenerating enzyme helps to strengthen and sustain light output. |
BBa_K325109 |
Photinus pyralis LRE and luciferase under pBADThis part is the part above expressed under pBAD for characterisation. |
BBa_K325209 |
L. cruciata LRE and luciferase (wildtype) under pBADThis part combines the Luciferin Regenerating Enzyme and luciferase from the Japanese firefly, Luciola cruciata. It is expressed under pBAD. |
BBa_K325229 |
L. cruciata LRE and luciferase (green) under pBADThis is the same as the part above but with a Val239Ile mutation which green-shifts its emission spectrum. |
BBa_K325239 |
L. cruciata LRE and luciferase (red) under pBADThis is the same as the part above but instead has a Gly326Ser mutation which red-shifts its emission spectrum. |
BBa_K325249 |
L. cruciata LRE and luciferase (scarlet) under pBADThis is the same as the part above but instead has a His433Tyr mutation which red-shifts its emission spectrum. |
BBa_K325259 |
L. cruciata LRE and luciferase (yellow) under pBADThis is the same as the part above but instead has a Pro452Ser mutation which shifts its emission spectrum to peak at a yellow wavelength. |
Summary table
<groupparts>iGEM010 Cambridge</groupparts>