Difference between revisions of "Part:BBa K2306003"
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<html><img style="float:left;width:64px;margin-right:2em" src="https://static.igem.wiki/teams/4765/wiki/2023-b-home.png" alt="contributed by Fudan iGEM 2023"></html>
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===Improved by Fudan iGEM 2023 ===
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This part is an effective anti-desiccation protein, and we compared it with ''H. ex'' mtSSB, finding that both proteins exhibit considerable desiccation resistance. Furthermore, when co-expressed with the antifreeze protein AnAFP and the desiccation-resistant protein, ''E. coli'' demonstrated higher desiccation resistance when simultaneously expressing SAHS 33020 and ''H. ex'' mtSSB compared to expressing SAHS 33020 or ''H. ex'' mtSSB individually.
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===Improved Part===
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Our improved part is [https://parts.igem.org/Part:BBa_K4765126 BBa_K4765126 (ribozyme connected: H. ex mtSSB + SAHS 33020 + AnAFP)].
  
 
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<partinfo>BBa_K2306003 short</partinfo>
 
<partinfo>BBa_K2306003 short</partinfo>
  
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This Biobrick features the gene sequence that encodes for the production of the tardigrade intrinsically disordered protein (TDP) "SAHS 33020". This is one of the several heat soluble proteins found in the tardigrades responsible for the ability of these microscopic animals to survive in the harshest conditions. Upon desiccation, tardigrade proteins form a glass matrix capable of protecting other fragile biological components. Therefore, this tardigrade protein can be combined with other perishable biological material (e.g. proteins) to increase its stability against dehydration or even enable the possibility of stabilizing material with just a previous drying step.
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This Biobrick features the gene sequence that encodes for the production of the tardigrade intrinsically disordered protein (TDP) "SAHS 33020". This is one of the several heat soluble proteins found in the tardigrades responsible for the ability of these microscopic animals to survive the harshest conditions. Upon desiccation, tardigrade proteins form a glass matrix capable of protecting other fragile biological components. Therefore, this tardigrade protein can be combined with other perishable biological material (e.g. proteins) to increase its stability against dehydration or even enable the possibility of stabilizing material with just a previous drying step.
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This BioBrick is featured in the composite part [https://parts.igem.org/Part:BBa_K2306008 BBa_K2306008] combined with a T7 promoter [https://parts.igem.org/Part:BBa_I712074 BBa_R0010], a ribosome binding site [https://parts.igem.org/Part:BBa_K2306014 BBa_k2306014] and a double terminator [https://parts.igem.org/Part:BBa_B0015 BBa_B0015] to control its expression. Further information about our project can be found on our [http://2017.igem.org/Team:TUDelft/Results#TDP results page].
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 11:04, 12 October 2023

contributed by Fudan iGEM 2023

Improved by Fudan iGEM 2023

This part is an effective anti-desiccation protein, and we compared it with H. ex mtSSB, finding that both proteins exhibit considerable desiccation resistance. Furthermore, when co-expressed with the antifreeze protein AnAFP and the desiccation-resistant protein, E. coli demonstrated higher desiccation resistance when simultaneously expressing SAHS 33020 and H. ex mtSSB compared to expressing SAHS 33020 or H. ex mtSSB individually.

Improved Part

Our improved part is BBa_K4765126 (ribozyme connected: H. ex mtSSB + SAHS 33020 + AnAFP).


Secretory-abundant heat soluble protein 33020 (SAHS 33020)

This Biobrick features the gene sequence that encodes for the production of the tardigrade intrinsically disordered protein (TDP) "SAHS 33020". This is one of the several heat soluble proteins found in the tardigrades responsible for the ability of these microscopic animals to survive the harshest conditions. Upon desiccation, tardigrade proteins form a glass matrix capable of protecting other fragile biological components. Therefore, this tardigrade protein can be combined with other perishable biological material (e.g. proteins) to increase its stability against dehydration or even enable the possibility of stabilizing material with just a previous drying step. This BioBrick is featured in the composite part BBa_K2306008 combined with a T7 promoter BBa_R0010, a ribosome binding site BBa_k2306014 and a double terminator BBa_B0015 to control its expression. Further information about our project can be found on our [http://2017.igem.org/Team:TUDelft/Results#TDP results page].

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 BsaI site found at 117