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

(→‎fliC E. coli, flagellin C coding sequence (BbaK1951005))
 
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{{:Team:Aix-Marseille/Template-Top|Basic Part}}
 
{{:Team:Aix-Marseille/Template-Top|Basic Part}}
  
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==Mobilisation by a siderophore==
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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.
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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_ 
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=== '''desA, lysine decarboxylase coding sequence''' [http://parts.igem.org/Part:BBa_K1951000 BBa_K1951000]===
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==Mobilisation by a siderophore==  
  
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This DNA sequence codes 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.
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===desA, lysine decarboxylase coding sequence [http://parts.igem.org/Part:BBa_K1951000 BBa_K1951000]===
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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.
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==='''desB, monooxygenase coding sequence''' [http://parts.igem.org/Part:BBa_K1951001 BBa_K1951001]===
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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.
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This enzyme is also the first step in the production of desferrioxame B which is a siderophore.
  
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This sequence codes a 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.
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===desB, monooxygenase coding sequence [http://parts.igem.org/Part:BBa_K1951001 BBa_K1951001]===
  
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==='''desC, acyl transferase coding sequence''' [http://parts.igem.org/Part:BBa_K1951002 BBa_K1951002]===
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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.
  
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''desC'' is the coding sequence of 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.
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===desC, acyl transferase coding sequence [http://parts.igem.org/Part:BBa_K1951002 BBa_K1951002]===
  
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==='''desD, Desferrioxamine biosynthesis coding sequence''' [http://parts.igem.org/Part:BBa_K1951003 BBa_K1951003]===
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''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.
  
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This coding sequence codes 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).
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===desD, Desferrioxamine biosynthesis coding sequence [http://parts.igem.org/Part:BBa_K1951003 BBa_K1951003]===
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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==
 
==Biosorption==
  
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=== '''fliC ''E. coli'', flagellin C coding sequence''' [http://parts.igem.org/Part:BBa_K1951005 BBa_K1951005]===
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=== fliC ''E. coli'', flagellin coding sequence  [http://parts.igem.org/Part:BBa_K1951005 BBa_K1951005]===
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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.
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It has been demonstrated that flagellin has the ability to adsorb precious metal such as platinum or gold.
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===fliC ''Desulfovibrio vulgaris'', flagellin coding sequence [http://parts.igem.org/Part:BBa_K1951006 BBa_K1951006]===
  
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This coding sequence codes the 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. This sequence is conserved in many bacterial strains. It has been demonstrated that Flagellin C has the ability to adsorb precious metal such as platinum or gold.
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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.
  
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===fliC Desulfovibrio, flagellin C coding sequence  (BbaK1951006)===
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===CsgA, curlin coding sequence  [http://parts.igem.org/Part:BBa_K1951007 BBa_K1951007]===
  
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This coding sequence codes 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, Platinum..  
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[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.
  
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=== CsgA, curlin coding sequence  (BbaK1951007)===
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<references/>
  
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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.
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{{:Team:Aix-Marseille/Template-Footer}}

Latest revision as of 23:29, 19 October 2016