Team:UQ-Australia/Parts

From 2009.igem.org

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(→Our Standard Parts)
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We have developed four parts so far that are in the registry. The physical DNA and sequence data is yet to be finalised.  
We have developed four parts so far that are in the registry. The physical DNA and sequence data is yet to be finalised.  
 +
''BBa_K205000''
''BBa_K205000''
 +
'''Name''': GroEL
'''Name''': GroEL
 +
'''Standard''': 21
'''Standard''': 21
 +
'''Function''': GroEL is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroES, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.
'''Function''': GroEL is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroES, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.
 +
''BBa_K205001''
''BBa_K205001''
 +
'''Name''': GroES
'''Name''': GroES
 +
'''Standard''': 21
'''Standard''': 21
 +
'''Function''': GroES is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroEL, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.
'''Function''': GroES is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroEL, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.
 +
''BBa_K205002''
''BBa_K205002''
 +
'''Name''': DnaK
'''Name''': DnaK
 +
'''Standard''': 23
'''Standard''': 23
 +
'''Function''': In conjuction with DnaJ and GrpE, DnaK assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaJ, GrpE, GroEL and GroES forms the heat shock system in bacteria.
'''Function''': In conjuction with DnaJ and GrpE, DnaK assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaJ, GrpE, GroEL and GroES forms the heat shock system in bacteria.
 +
''BBa_K205003''
''BBa_K205003''
 +
'''Name''': DnaJ and GrpE
'''Name''': DnaJ and GrpE
 +
'''Standard''':23
'''Standard''':23
 +
'''Function''': In conjuction with DnaK and GrpE, DnaJ assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaK, GrpE, GroEL and GroES forms the heat shock system in bacteria.
'''Function''': In conjuction with DnaK and GrpE, DnaJ assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaK, GrpE, GroEL and GroES forms the heat shock system in bacteria.
Note that GrpE is used to catalyse the dephosphorylation of ATP to ADP, and changes the protein conformation of the DnaK/DnaJ complex to faciliate efficient polypeptide folding.
Note that GrpE is used to catalyse the dephosphorylation of ATP to ADP, and changes the protein conformation of the DnaK/DnaJ complex to faciliate efficient polypeptide folding.
 +
We are currently working on developing standard parts to add to the registry for the Ag43 aggregation gene and the MerR mercury resistance operon repressor.
We are currently working on developing standard parts to add to the registry for the Ag43 aggregation gene and the MerR mercury resistance operon repressor.

Revision as of 00:56, 14 October 2009


Our Standard Parts

BioPrecipitation

We have developed four parts so far that are in the registry. The physical DNA and sequence data is yet to be finalised.


BBa_K205000


Name: GroEL

Standard: 21

Function: GroEL is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroES, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.


BBa_K205001


Name: GroES

Standard: 21

Function: GroES is a chaperone protein that is responsible for the prevention of polypeptide mis-folding. In conjunction with GroEL, these two subunits form an assembly dimer that are promote efficient protein folding, especially under stressful conditions such as heat shock. This chaperone protein belongs to the eukaryotic HSP60 (heat shock protein) family.


BBa_K205002


Name: DnaK

Standard: 23

Function: In conjuction with DnaJ and GrpE, DnaK assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaJ, GrpE, GroEL and GroES forms the heat shock system in bacteria.


BBa_K205003


Name: DnaJ and GrpE

Standard:23

Function: In conjuction with DnaK and GrpE, DnaJ assists in correct polypeptide folding and is the Prokaryotic homologue of the Eukaryotic chaperone system 'Hsp70'. This gene, along with DnaK, GrpE, GroEL and GroES forms the heat shock system in bacteria. Note that GrpE is used to catalyse the dephosphorylation of ATP to ADP, and changes the protein conformation of the DnaK/DnaJ complex to faciliate efficient polypeptide folding.


We are currently working on developing standard parts to add to the registry for the Ag43 aggregation gene and the MerR mercury resistance operon repressor.

Retrieved from "http://2009.igem.org/Team:UQ-Australia/Parts"