Team:UQ-Australia/Parts

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Latest revision as of 00:27, 22 October 2009

BioPrecipitation

We have developed four parts so far that are in the registry. The physical DNA and sequence data is yet to be finalised. The four parts used in this project were sent to our lab by Christos Kyratsous from Columbia University, we thank you for your contribution.

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.

[http://partsregistry.org/Part:BBa_K205000 Get this part]

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.

[http://partsregistry.org/Part:BBa_K205001 Get this part]

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.

[http://partsregistry.org/Part:BBa_K205002 Get this part]

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.

[http://partsregistry.org/Part:BBa_K205003 Get this part]

Bioaccumulation

BBa_K205004

Name: MerT

Standard: 23 Assembly in BBa_J63010

Source: Professor David Wilson, of the Department of Molecular Biology and Genetics, Cornell University.

Function: MerT facilitates the transport of Hg(II) across the bacterial inner membrane, and enhances uptake of mercury from the environment. In combination with MerP, a periplasmic mercury binding protein which ferries mercury to MerT, these two proteins can greatly increase the intracellular accumulation of mercury. MerT is part of the endogenous Mer operon which many bacterial species use to detoxify various forms of mercury.

[http://partsregistry.org/Part:BBa_K205004 Get this part]

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 			<a href="https://2009.igem.org/Team:UQ-Australia/Lab" style="color: white">Our Lab
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-=='''Title'''==
-'''Sub-header'''
-Text
+== '''BioPrecipitation''' ==
+We have developed four parts so far that are in the registry. The physical DNA and sequence data is yet to be finalised. The four parts used in this project were sent to our lab by Christos Kyratsous from Columbia University, we thank you for your contribution.
+''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.
+[http://partsregistry.org/Part:BBa_K205000 '''Get this part''']
+''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.
+[http://partsregistry.org/Part:BBa_K205001 '''Get this part''']
+''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.
+[http://partsregistry.org/Part:BBa_K205002 '''Get this part''']
+''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.
+[http://partsregistry.org/Part:BBa_K205003 '''Get this part''']
+=='''Bioaccumulation'''==
+''BBa_K205004''
+'''Name:''' MerT
+'''Standard:''' 23 Assembly in BBa_J63010
+'''Source:''' Professor David Wilson, of the Department of Molecular Biology and Genetics, Cornell University.
+'''Function:''' MerT facilitates the transport of Hg(II) across the bacterial inner membrane, and enhances uptake of mercury from the environment. In combination with MerP, a periplasmic mercury binding protein which ferries mercury to MerT, these two proteins can greatly increase the intracellular accumulation of mercury. MerT is part of the endogenous Mer operon which many bacterial species use to detoxify various forms of mercury.
+[http://partsregistry.org/Part:BBa_K205004 '''Get this part''']