Difference between revisions of "Part:BBa K3739010"

 
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<partinfo>BBa_K3739010 short</partinfo>
 
<partinfo>BBa_K3739010 short</partinfo>
  
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LMT is a signal peptide from the lytic murein transglycosylase of  V.natriegens and GFP can show the secretion effciency of LMT
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This part contains a ''Vibrio natriegens-optimized'' GFP coding sequence, and the GFP is fused at N-terminal with his-tag in order to let us purify the protein. His-GFP is fused with secretory peptide from LMT.We use <partinfo>BBa_K3739010</partinfo> to construct the expression system and help prove the function of some signal peptide.
  
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===Biology===
  
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LMT
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===Usage and Biology===
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Lytic murein transglycosylase (LMT) is an enzyme which is able to degrade murein, a component of cell wall of bacteria. There are two kind of LMTs existing in ''E.coli'': the membrane-binding one and the soluble one. The gene coding LMT homolog is also incorporated in the genome of ''Vibrio natriegens''. The LMT signal peptide (named LMT in our parts) is from the LMT homolog, which can lead the fused protein secreted out of ''Vibrio natriegens''.
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GFP
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Protein tags are peptides genetically fused to the proteins of interest. There are many different kinds of tags developed for for different purposes. For labeling experiments, normally the proteins of interest are tagged directly by fluorescent tags. Green fluorescent protein (GFP) make it easier to study protein localization, interactions and dynamics when fusing with other peptides and proteins.
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===Usage===
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Here, we used <partinfo>BBa_Kxxxx</partinfo> to construct the expression system and obtained the composite part <partinfo>BBa_Kxxxx. We transformed the constructed plasmid on the expression vector pET-28a (+) into V. ''natriegens'' to extract the protein. This protein work together with those from <partinfo>BBa_Kxxxx</partinfo> and <partinfo>BBa_Kxxxx</partinfo> to verify the function of our secretory peptides Aly01 and LMT.
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===Characterization===
  
 
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Revision as of 23:14, 21 October 2021


LMT-his-GFP

This part contains a Vibrio natriegens-optimized GFP coding sequence, and the GFP is fused at N-terminal with his-tag in order to let us purify the protein. His-GFP is fused with secretory peptide from LMT.We use BBa_K3739010 to construct the expression system and help prove the function of some signal peptide.

Biology

LMT

Lytic murein transglycosylase (LMT) is an enzyme which is able to degrade murein, a component of cell wall of bacteria. There are two kind of LMTs existing in E.coli: the membrane-binding one and the soluble one. The gene coding LMT homolog is also incorporated in the genome of Vibrio natriegens. The LMT signal peptide (named LMT in our parts) is from the LMT homolog, which can lead the fused protein secreted out of Vibrio natriegens.

GFP

Protein tags are peptides genetically fused to the proteins of interest. There are many different kinds of tags developed for for different purposes. For labeling experiments, normally the proteins of interest are tagged directly by fluorescent tags. Green fluorescent protein (GFP) make it easier to study protein localization, interactions and dynamics when fusing with other peptides and proteins.

Usage

Here, we used No part name specified with partinfo tag. to construct the expression system and obtained the composite part No part name specified with partinfo tag. and No part name specified with partinfo tag. to verify the function of our secretory peptides Aly01 and LMT.

Characterization

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 SapI.rc site found at 133