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Team:UQ-Australia/Parts
From 2009.igem.org
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.
