Difference between revisions of "Team:Aix-Marseille/Basic Part"

Revision as of 16:35, 19 October 2016

Mobilisation by a siderophore

You will find on this page the basic parts which have been designed by our team. For further details, you can also go on http://www.parts.igem.org and have a look to the biobrick reference BBa_

desA, lysine decarboxylase coding sequence [http://parts.igem.org/Part:BBa_K1951000 BBa_K1951000]

This DNA sequence codes [http://metacyc.org/gene?orgid=META&id=SCO2782 Lysine descarboxylase] (Streptomyces) is an enzyme from the lyase family that converts lysine to cadaverin. The enzyme realizes the carbonyl group of the lysin amino acid. There is cadeverin producing (1,5-diaminopentane), a primary diamine which alkaline environment. The lysine decarboxylase is an enzyme induced the synthesis of which is promoted by anaerobiosis and an acidic pH. In bacteriology, this enzyme is sought through the middle of Moeller lysine or medium lysine Taylor. This enzyme is also the first step in the production of desferrioxame B which is a siderophore.

desB, monooxygenase coding sequence [http://parts.igem.org/Part:BBa_K1951001 BBa_K1951001]

This sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2783-MONOMER monooxygenase] which is an enzyme that incorporate one hydroxyl group into substrates in many metabolic pathways. In this reaction, the two atoms of dioxygen are reduced to one hydroxyl and one H2O molecule by the concomitant oxidation of NAD(P)H. It is also the second step in the production of Desferrioxamine B in Streptomyces, allowing the transformation of cadeverine into N-hydroxycadaverine.

desC, acyl transferase coding sequence [http://parts.igem.org/Part:BBa_K1951002 BBa_K1951002]

desC is the coding sequence of [http://metacyc.org/gene?orgid=META&id=SCO2784-MONOMER DesC] which is an acyl transferase of the Desferrioxamine production pathway. It is the enzyme of the third step that transform N-hydroxycadaverin into N-acetyl N-hydroxucadaverine by an Acetyl-CoA dependent manner.

desD, Desferrioxamine biosynthesis coding sequence [http://parts.igem.org/Part:BBa_K1951003 BBa_K1951003]

This coding sequence codes [http://metacyc.org/gene?orgid=META&id=SCO2785-MONOMER DesD] of Streptomyces coelicolor, which is the last protein involved in the metabolic pathway of Desferrioxamine B. This enzyme is called Desferrioxamine biosynthesis protein or DesD and allows to transform N-acetyl N-hydroxycadaverine into Desferrioxamine B (by the transformation of 3 nucleoside triphosphate into 3 nucleoside 5'monophosphate-3-diphosphate).

Biosorption

fliC E. coli, flagellin C coding sequence [http://parts.igem.org/Part:BBa_K1951005 BBa_K1951005], improvement of [http://parts.igem.org/Part:BBa_K1463604 BBa_K1463604 (Glasgow 2014)]

This coding sequence codes the [http://ecocyc.org/gene?orgid=ECOLI&id=EG10321-MONOMER Flagellin C (FliC)] protein from Escherichia coli strain. FliC is the main protein constitutive of the flagelar filament and is involved to promote bacterial swimming. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as platinum or gold.

fliC Desulfovibrio, flagellin C coding sequence [http://parts.igem.org/Part:BBa_K1951006 BBa_K1951006]

This coding sequence codes [http://ecocyc.org/gene?orgid=DVUL882&id=GJIL-3010-MONOMER flagellin C] which is a main protein involved for the extracellular flagellar establishment. Flagellar enables bacterial swimming. It has been shown that the flagellin structure from Desulfovibrio vulgaris strain Hildenborough can adsorb metallic nanoparticules as gold or platinum.

CsgA, curlin coding sequence [http://parts.igem.org/Part:BBa_K1951007 BBa_K1951007]

[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many Enterobacteriaceae. Curli were first discovered in the late 1980s on Escherichia coli strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of E. coli and Salmonella spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. It has been shown that Curli can bind some metals ^[1] and that why we wanted to use it in our project.

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 ===CsgA, curlin coding sequence  [http://parts.igem.org/Part:BBa_K1951007 BBa_K1951007]===
-[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many ''Enterobacteriaceae''. Curli were first discovered in the late 1980s on ''Escherichia coli'' strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of ''E. coli'' and ''Salmonella'' spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response.
+[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli are coiled surface structures that assemble preferentially at growth temperatures below 37 degrees Celsius. Curli are the major proteinaceous component of a complex extracellular matrix produced by many ''Enterobacteriaceae''. Curli were first discovered in the late 1980s on ''Escherichia coli'' strains that caused bovine mastitis, and have since been implicated in many physiological and pathogenic processes of ''E. coli'' and ''Salmonella'' spp. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation. Curli also mediate host cell adhesion and invasion, and they are potent inducers of the host inflammatory response. It has been shown that Curli can bind some metals <ref name="metal_adhesion">[http://www.nature.com.sci-hub.cc/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga Department of Health Sciences and Technology, ETH Zurich, Schmelzbergstrasse 9, Zurich 8092, Switzerland.]</ref> and that why we wanted to use it in our project.
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Difference between revisions of "Team:Aix-Marseille/Basic Part"

Revision as of 16:35, 19 October 2016

Contents

Basic Part