Difference between revisions of "Part:BBa K185049"
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The ATP-dependent Lon protease is a member of the AAA+ family of proteins (ATPases associated with various cellular activities), which is present in archaea, prokaryotes and eukaryotic mitochondria, peroxisomes and plastids. Lon has multiple cellular functions such as degrading abnormal polypeptides, as well as certain regulatory proteins and metabolic enzymes, acting as a chaperone and binding to nucleic acids. | The ATP-dependent Lon protease is a member of the AAA+ family of proteins (ATPases associated with various cellular activities), which is present in archaea, prokaryotes and eukaryotic mitochondria, peroxisomes and plastids. Lon has multiple cellular functions such as degrading abnormal polypeptides, as well as certain regulatory proteins and metabolic enzymes, acting as a chaperone and binding to nucleic acids. | ||
In our project, since the Lon protease can hydrolysis RelB protein efficiently, we use it to balance the concentration of relE and relB inside E.coli. | In our project, since the Lon protease can hydrolysis RelB protein efficiently, we use it to balance the concentration of relE and relB inside E.coli. | ||
| + | However, the original part we have provided contains a PstI restriction site in Lon sequence.If you want to use this part. You can cut it with SpeI site instead of PstI. Or you can utilize another part '''BBa_K185050''', which is a PstI-mutated Lon coding sequence(with no PstI site). | ||
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<!-- Add more about the biology of this part here | <!-- Add more about the biology of this part here | ||
===Usage and Biology=== | ===Usage and Biology=== | ||
Latest revision as of 13:35, 17 October 2009
Lon protease
The ATP-dependent Lon protease is a member of the AAA+ family of proteins (ATPases associated with various cellular activities), which is present in archaea, prokaryotes and eukaryotic mitochondria, peroxisomes and plastids. Lon has multiple cellular functions such as degrading abnormal polypeptides, as well as certain regulatory proteins and metabolic enzymes, acting as a chaperone and binding to nucleic acids. In our project, since the Lon protease can hydrolysis RelB protein efficiently, we use it to balance the concentration of relE and relB inside E.coli. However, the original part we have provided contains a PstI restriction site in Lon sequence.If you want to use this part. You can cut it with SpeI site instead of PstI. Or you can utilize another part BBa_K185050, which is a PstI-mutated Lon coding sequence(with no PstI site).
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 619
- 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 619
- 21INCOMPATIBLE WITH RFC[21]Illegal BamHI site found at 1332
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 619
- 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 619
Illegal AgeI site found at 1795
Illegal AgeI site found at 1879
Illegal AgeI site found at 2077
Illegal AgeI site found at 2110 - 1000COMPATIBLE WITH RFC[1000]