Difference between revisions of "Part:BBa K538000"

 
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<partinfo>BBa_K538000 short</partinfo>
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===Cpn10 (''O. antarctica'')===
  
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This part encodes the protein ''cochaperonin 10'', which is part of the Cpn10/Cpn60 chaperonin system of ''Oleispira antarctica''.
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[[Image:Cpn10-60_graphs.gif|right|frame|Figure 1: (a) ''E. coli'' 's growth rate as a function of temperature, in strains that do (white circles) or do not (black circles) express ''Cpn60/10'', and (b) ''in vitro'' refolding activities of ''Cpn60/10'' as a function of temperature (black circles), compared with that of ''E. coli'' 's endogenous ''GroEL/ES'' (white circles). '''Adapted from Ferrer ''et al.'' (2003)''']]
  
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[More information will follow soon.]
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This BioBrick encodes the protein ''cochaperonin 10'', which is part of the ''Cpn60/10'' chaperone system of ''Oleispira antarctica''. When coexpressed with ''chaperonin 60'' (''Cpn60'', [[Part:BBa_K538001 | BBa_K538001]]), it forms a heteromultimer that can refold enzymes at very low temperatures, thus safeguarding their functionality. This has been shown to enable ''E. coli'' to grow even at freezing point. (Figure 1)
  
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===Usage and Biology===
 
===Usage and Biology===
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''Cpn10'' and ''Cpn60'' are, respectively, homologous to ''GroES'' and ''GroEL'' of ''E. coli''. The ''GroEL/ES'' chaperone system promotes the folding and/or assembly of over 30% of ''E. coli'''s cellular proteins, is required for bacteriophage morphogenesis and has a role in protein secretion.[http://www.nature.com/nature/journal/v355/n6355/abs/355033a0.html][http://onlinelibrary.wiley.com/doi/10.1002/1521-3773%2820020402%2941:7%3C1098::AID-ANIE1098%3E3.0.CO;2-9/abstract] However, it rapidly loses its refolding activity at temperatures below 37°C. (Figure 1b)[http://www.nature.com/nbt/journal/v21/n11/full/nbt1103-1266b.html] ''Cpn60/10'', on the other hand, functions very well at these temperatures.
  
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Ferrer ''et al.'' demonstrated that ''Cpn60'''s product, ''chaperonin 60'', coprecipitates with many of the genes found in the proteome of ''E. coli''.[http://onlinelibrary.wiley.com/doi/10.1002/pmic.200500031/abstract] Also, by transforming ''E. coli'' with ''Cpn10'' and ''Cpn60'', they've enabled it to grow even at freezing point. (Figure 1a)
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<span class='h3bb'>Sequence and Features</span>
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[Under construction]
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===Sequence and Features===
 
<partinfo>BBa_K538000 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K538000 SequenceAndFeatures</partinfo>
  
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===References===
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# '''Gething & Sambrook''' Protein folding in the cell, ''Nature 355, 33–45'' (1992)
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# '''Walter & Buchner''' Molecular Chaperones — Cellular Machines for Protein Folding, ''Angew. Chem. Int. Ed. Eng. 41, 1098–1113'' (2002)
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# '''Ferrer ''et al.''''' Chaperonins govern growth of ''Escherichia coli'' at low temperatures, ''Nat. Biotech. 21, 1266 - 1267'' (2003)
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# '''Strocchi, Ferrer, Timmis & Golyshin''' Low temperature-induced systems failure in ''Escherichia coli'': Insights from rescue by cold-adapted chaperones, ''Proteomics 6 (1), 193-206'' (2005)
  
 
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Revision as of 12:05, 29 July 2011

Cpn10 (O. antarctica)

Figure 1: (a) E. coli 's growth rate as a function of temperature, in strains that do (white circles) or do not (black circles) express Cpn60/10, and (b) in vitro refolding activities of Cpn60/10 as a function of temperature (black circles), compared with that of E. coli 's endogenous GroEL/ES (white circles). Adapted from Ferrer et al. (2003)

This BioBrick encodes the protein cochaperonin 10, which is part of the Cpn60/10 chaperone system of Oleispira antarctica. When coexpressed with chaperonin 60 (Cpn60, BBa_K538001), it forms a heteromultimer that can refold enzymes at very low temperatures, thus safeguarding their functionality. This has been shown to enable E. coli to grow even at freezing point. (Figure 1)

Usage and Biology

Cpn10 and Cpn60 are, respectively, homologous to GroES and GroEL of E. coli. The GroEL/ES chaperone system promotes the folding and/or assembly of over 30% of E. coli's cellular proteins, is required for bacteriophage morphogenesis and has a role in protein secretion.[http://www.nature.com/nature/journal/v355/n6355/abs/355033a0.html][http://onlinelibrary.wiley.com/doi/10.1002/1521-3773%2820020402%2941:7%3C1098::AID-ANIE1098%3E3.0.CO;2-9/abstract] However, it rapidly loses its refolding activity at temperatures below 37°C. (Figure 1b)[http://www.nature.com/nbt/journal/v21/n11/full/nbt1103-1266b.html] Cpn60/10, on the other hand, functions very well at these temperatures.

Ferrer et al. demonstrated that Cpn60's product, chaperonin 60, coprecipitates with many of the genes found in the proteome of E. coli.[http://onlinelibrary.wiley.com/doi/10.1002/pmic.200500031/abstract] Also, by transforming E. coli with Cpn10 and Cpn60, they've enabled it to grow even at freezing point. (Figure 1a)

[Under construction]


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    INCOMPATIBLE WITH RFC[1000]
    Illegal BsaI.rc site found at 52


References

  1. Gething & Sambrook Protein folding in the cell, Nature 355, 33–45 (1992)
  2. Walter & Buchner Molecular Chaperones — Cellular Machines for Protein Folding, Angew. Chem. Int. Ed. Eng. 41, 1098–1113 (2002)
  3. Ferrer et al. Chaperonins govern growth of Escherichia coli at low temperatures, Nat. Biotech. 21, 1266 - 1267 (2003)
  4. Strocchi, Ferrer, Timmis & Golyshin Low temperature-induced systems failure in Escherichia coli: Insights from rescue by cold-adapted chaperones, Proteomics 6 (1), 193-206 (2005)