Difference between revisions of "Part:BBa K5184022"

 
Line 3: Line 3:
 
<partinfo>BBa_K5184022 short</partinfo>
 
<partinfo>BBa_K5184022 short</partinfo>
  
−
"G1M5 is the mutated, less hydrophobic version of the signal peptide of the G1 cyclomaltodextrin glucanotransferase (CGtase) of Bacillus sp., which allows the extracellular secretion of the bacterial enzyme. The signal peptide can be divided into three regions: an N-terminus region with several positively charged amino acids, a central hydrophobic region, and a hydrophilic cleavage region. The N-terminus region was found to act as intramolecular chaperones, and to be in cooperation with SecA and SecB to act as factors for protein targeting to the membrane.
+
G1M5 is the mutated, less hydrophobic version of the signal peptide of the G1 cyclomaltodextrin glucanotransferase (CGtase) of Bacillus sp., which allows the extracellular secretion of the bacterial enzyme. The signal peptide can be divided into three regions: an N-terminus region with several positively charged amino acids, a central hydrophobic region, and a hydrophilic cleavage region. The N-terminus region was found to act as intramolecular chaperones, and to be in cooperation with SecA and SecB to act as factors for protein targeting to the membrane.
  
 
Constructs containing the signal peptide G1M5 allows extracellular secretion of the fusion protein. In context of our project this will allow export of spider venom peptide into extraceullar spaceafter translation in cytoplasm, of which can lower production cost and make production process more efficient. This exporting process can also provide a more oxidative environment that aids the formation of disulphide bridges that is essential for the correct folding of spider venom peptides."
 
Constructs containing the signal peptide G1M5 allows extracellular secretion of the fusion protein. In context of our project this will allow export of spider venom peptide into extraceullar spaceafter translation in cytoplasm, of which can lower production cost and make production process more efficient. This exporting process can also provide a more oxidative environment that aids the formation of disulphide bridges that is essential for the correct folding of spider venom peptides."

Revision as of 10:12, 27 September 2024


G1M5-SUMO-tag

G1M5 is the mutated, less hydrophobic version of the signal peptide of the G1 cyclomaltodextrin glucanotransferase (CGtase) of Bacillus sp., which allows the extracellular secretion of the bacterial enzyme. The signal peptide can be divided into three regions: an N-terminus region with several positively charged amino acids, a central hydrophobic region, and a hydrophilic cleavage region. The N-terminus region was found to act as intramolecular chaperones, and to be in cooperation with SecA and SecB to act as factors for protein targeting to the membrane.

Constructs containing the signal peptide G1M5 allows extracellular secretion of the fusion protein. In context of our project this will allow export of spider venom peptide into extraceullar spaceafter translation in cytoplasm, of which can lower production cost and make production process more efficient. This exporting process can also provide a more oxidative environment that aids the formation of disulphide bridges that is essential for the correct folding of spider venom peptides."

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
    COMPATIBLE WITH RFC[1000]