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

Latest revision as of 23:29, 19 October 2016

Mobilisation by a siderophore

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

This DNA sequence codes a [http://metacyc.org/gene?orgid=META&id=SCO2782 Lysine decarboxylase] (Streptomyces coelicolor) which is an enzyme from the lyase family that converts lysine into cadaverine. The enzyme releases the carbonyl group of the lysin amino acid. Cadaverine (or 1,5-diaminopentane) is a primary diamine which renders the medium alkaline. The lysine decarboxylase is an enzyme whose synthesis is promoted by anaerobiosis and an acidic pH. 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 incorporates 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 transforms 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 the conversion of 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 coding sequence [http://parts.igem.org/Part:BBa_K1951005 BBa_K1951005]

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

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

This sequence codes for the [http://ecocyc.org/gene?orgid=DVUL882&id=GJIL-3010-MONOMER flagellin] protein (FliC) from Desulfovibrio vulgaris which is the main protein involved for making the extracellular flagellum. Flagella are used by bacteria for swimming. It has been shown that the flagella 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 fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation ^[1]. It has been shown that amyloid proteins, like curli, can bind some metals ^[2] and thats why we wanted to use it in our project.

↑ Michelle M. Barnhart and Matthew R. Chapman 2010, Annual Review of Microbiology

↑ [http://www.nature.com/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga 2016, Nature Nanotechnology]

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 {{:Team:Aix-Marseille/Template-Top|Basic Part}}
-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 parts page] and have a look to the corresponding BioBrick's page.
+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://parts.igem.org/Main_Page parts page] and have a look to the corresponding BioBrick's page.
 ==Mobilisation by a siderophore==
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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 fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation <ref name="Curli">[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838481/ Michelle M. Barnhart and Matthew R. Chapman]</ref>. It has been shown that amyloid proteins, like curli, can bind some metals <ref name="metal_adhesion">[http://www.nature.com/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga 2016, Nature Nanotechnology]</ref> and thats why we wanted to use it in our project.
+[http://ecocyc.org/gene?orgid=ECOLI&id=EG11489-MONOMER CsgA] is the major and structural subunit of the curli fimbriae. Curli fibers are involved in adhesion to surfaces, cell aggregation, and biofilm formation <ref name="Curli">[https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2838481/ Michelle M. Barnhart and Matthew R. Chapman 2010, Annual Review of Microbiology]</ref>. It has been shown that amyloid proteins, like curli, can bind some metals <ref name="metal_adhesion">[http://www.nature.com/nnano/journal/v11/n4/full/nnano.2015.310.html Sreenath Bolisetty and Raffaele Mezzenga 2016, Nature Nanotechnology]</ref> and thats why we wanted to use it in our project.
 <references/>
 {{:Team:Aix-Marseille/Template-Footer}}

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

Latest revision as of 23:29, 19 October 2016

Contents

Basic Part