Difference between revisions of "Team:MIT/Basic Part"

 
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Basic Parts
 
Basic Parts
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Team MIT has chosen our cpComE-NLS-VP16-NES SM6 construct to share as our best part. This part contains a human optimized coding sequence for a constitutively phosphorylated ComE, the putative response regulator protein for the ComCDE two-component signaling pathway, native to Streptococcus mutans strain SM6 (a bacteria common in the human oral cavity). Design elements were chosen to optimize expression and function of ComE in human cells. The aspartic acid at amino acid position 60 (the putative phosphorylation site of the response regulator) in a wildtype ComE was changed to a glutamic acid, to act as a phosphomimetic.  
 
Team MIT has chosen our cpComE-NLS-VP16-NES SM6 construct to share as our best part. This part contains a human optimized coding sequence for a constitutively phosphorylated ComE, the putative response regulator protein for the ComCDE two-component signaling pathway, native to Streptococcus mutans strain SM6 (a bacteria common in the human oral cavity). Design elements were chosen to optimize expression and function of ComE in human cells. The aspartic acid at amino acid position 60 (the putative phosphorylation site of the response regulator) in a wildtype ComE was changed to a glutamic acid, to act as a phosphomimetic.  
 
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Normally, to be used as part of a functional sensing system, the ComE response regulator must be paired with the ComD histidine kinase receptor protein. When ComD binds to the S. mutans competence stimulating peptide, it autophosphorylates and transfers a phosphate group to an aspartic acid on ComE, enabling ComE to oligomerize and bind to specific DNA sequences to promote transcription. This constitutively phosphorylated ComE should theoretically always be able to bind DNA. The cpComE coding sequence is fused to a nuclear localization sequence (NLS), VP16 activating domain, and a nuclear export sequence (NES). It is in a pSB1C3 backbone and is BioBrick and MoClo compatible.
 
Normally, to be used as part of a functional sensing system, the ComE response regulator must be paired with the ComD histidine kinase receptor protein. When ComD binds to the S. mutans competence stimulating peptide, it autophosphorylates and transfers a phosphate group to an aspartic acid on ComE, enabling ComE to oligomerize and bind to specific DNA sequences to promote transcription. This constitutively phosphorylated ComE should theoretically always be able to bind DNA. The cpComE coding sequence is fused to a nuclear localization sequence (NLS), VP16 activating domain, and a nuclear export sequence (NES). It is in a pSB1C3 backbone and is BioBrick and MoClo compatible.
 
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Please find below the list of all of our basic parts!
 
Please find below the list of all of our basic parts!
 
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Latest revision as of 02:02, 18 October 2018

Home
Team
Team Members Collaborations
Project
Design Results InterLab Notebook Protocols Attributions
Parts
Basic Parts Composite Parts
Safety
Human Practices
Integrated Human Practices Public Engagement
Model
Basic Parts
Team MIT has chosen our cpComE-NLS-VP16-NES SM6 construct to share as our best part. This part contains a human optimized coding sequence for a constitutively phosphorylated ComE, the putative response regulator protein for the ComCDE two-component signaling pathway, native to Streptococcus mutans strain SM6 (a bacteria common in the human oral cavity). Design elements were chosen to optimize expression and function of ComE in human cells. The aspartic acid at amino acid position 60 (the putative phosphorylation site of the response regulator) in a wildtype ComE was changed to a glutamic acid, to act as a phosphomimetic.
Normally, to be used as part of a functional sensing system, the ComE response regulator must be paired with the ComD histidine kinase receptor protein. When ComD binds to the S. mutans competence stimulating peptide, it autophosphorylates and transfers a phosphate group to an aspartic acid on ComE, enabling ComE to oligomerize and bind to specific DNA sequences to promote transcription. This constitutively phosphorylated ComE should theoretically always be able to bind DNA. The cpComE coding sequence is fused to a nuclear localization sequence (NLS), VP16 activating domain, and a nuclear export sequence (NES). It is in a pSB1C3 backbone and is BioBrick and MoClo compatible.
Please find below the list of all of our basic parts!
Name Type Description
BBa_K2649001 Coding cpComE-NLS-VP16-NES SM6
BBa_K2649000 Coding ComE-NLS-VP16-NES SM6
BBa_K2649004 Coding ComE-NLS-VP16-NES NN2025
BBa_K2649005 Coding cpComE-NLS-VP16-NES NN2025
BBa_K2649010 Coding cpComE-NLS-VP16-NES UA159
BBa_K2649011 coding eComE-NLS-VP16-NES
BBa_K2649006 Regulatory ComE Binding Promoter Low Affinity
BBa_K2649007 Regulatory ComE Binding Promoter Med Affinity
BBa_K2649008 Coding CD4-ComD-mKO2 NN2025
BBa_K2649009 Coding CD4-ComD-mKO2 UA159
BBa_K2649002 Backbone Phytobricks Universal Backbone with RFP TU Insert
BBa_K2649003 Backbone pSB1K3 with RFP TU Insert