Difference between revisions of "Part:BBa K2350018"

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  Endolysin, also known as lysin or murein hydrolase, is peptidoglycan-hydrolyzing enzymes used by bacteriophages to degrade the bacterial host’s cell wall and lead to cell lysis. The gene sequences of endolysin in different species of bacteriophages are also slightly different. Most endolysin are monomeric proteins and consist of two types of domains, enzymatically active domains (EADs) and cell-binding domains (CBDs). EAD cleaves peptidoglycan bond, and CBD binds to the host’s cell wall.  
 
  Endolysin, also known as lysin or murein hydrolase, is peptidoglycan-hydrolyzing enzymes used by bacteriophages to degrade the bacterial host’s cell wall and lead to cell lysis. The gene sequences of endolysin in different species of bacteriophages are also slightly different. Most endolysin are monomeric proteins and consist of two types of domains, enzymatically active domains (EADs) and cell-binding domains (CBDs). EAD cleaves peptidoglycan bond, and CBD binds to the host’s cell wall.  
  However, endolysin can’t pass through cytoplasmic membrane to access the cell wall alone. The lysis process includes another protein called holin, which can forms holes on cell membrane. In 2017 NYMU project, we combine endolysin and holin as suicide mechanism. You can see more information in BBa_2350019 for holin part, and BBa_2350020 for part containing both endolysin and holin.
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<br>  However, endolysin can’t pass through cytoplasmic membrane to access the cell wall alone. The lysis process includes another protein called holin, which can forms holes on cell membrane. In 2017 NYMU project, we combine endolysin and holin as suicide mechanism. You can see more information in BBa_2350019 for holin part, and BBa_2350020 for part containing both endolysin and holin.
  Besides endolysin, in this composite part, we choose BBa_J23106 as a constitutive promoter, BBa_B0034 as ribosome binding site, BBa_B0010 and BBa_B0012 as double terminator, all of which are widely used parts in iGEM.
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<br>  Besides endolysin, in this composite part, we choose BBa_J23106 as a constitutive promoter, BBa_B0034 as ribosome binding site, BBa_B0010 and BBa_B0012 as double terminator, all of which are widely used parts in iGEM.

Revision as of 08:16, 21 October 2017

  Endolysin, also known as lysin or murein hydrolase, is peptidoglycan-hydrolyzing enzymes used by bacteriophages to degrade the bacterial host’s cell wall and lead to cell lysis. The gene sequences of endolysin in different species of bacteriophages are also slightly different. Most endolysin are monomeric proteins and consist of two types of domains, enzymatically active domains (EADs) and cell-binding domains (CBDs). EAD cleaves peptidoglycan bond, and CBD binds to the host’s cell wall.
  However, endolysin can’t pass through cytoplasmic membrane to access the cell wall alone. The lysis process includes another protein called holin, which can forms holes on cell membrane. In 2017 NYMU project, we combine endolysin and holin as suicide mechanism. You can see more information in BBa_2350019 for holin part, and BBa_2350020 for part containing both endolysin and holin.
  Besides endolysin, in this composite part, we choose BBa_J23106 as a constitutive promoter, BBa_B0034 as ribosome binding site, BBa_B0010 and BBa_B0012 as double terminator, all of which are widely used parts in iGEM.