Difference between revisions of "Part:BBa K5115034"
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| − | csoS operon | + | <html><img style="float:right;width:128px" src="https://static.igem.wiki/teams/5115/czh/mineral-logo.svg" alt="contributed by Fudan iGEM 2024"></html> |
| + | __TOC__ | ||
| + | ===Introduction=== | ||
| + | The csoS operon, originating from the ''Halothiobacillus neapolitanus'', encodes a series of proteins essential for the assembly of α-carboxysomes, a type of microcompartment that facilitates the sequestration and concentration of enzymes involved in carbon fixation, particularly ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)<ref>Oltrogge, L. M., Chaijarasphong, T., Chen, A. W., Bolin, E. R., Marqusee, S., & Savage, D. F. (2020). Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. Nature structural & molecular biology, 27(3), 281–287. https://doi.org/10.1038/s41594-020-0387-7.</ref>. In literature, α-carboxysomes have been extensively studied and successfully utilized in ''Escherichia coli'' for enhancing carbon fixation efficiency and optimizing metabolic pathways. The csoS operon includes key structural proteins including csoS4B, csoS1C, csoS1A, csoS1B, csoS1D, csoS4A, and CsoS2, which play crucial roles in forming the shell and encapsulating cargo enzymes, including those required for hydrogen production. The operon serves as a model for synthetic biology applications, particularly in constructing reactors capable of enhancing catalytic functions through encapsulation of heterologous enzymes. The successful expression of this operon in ''E. coli'' demonstrates its potential for industrial and biotechnological applications, enabling the creation of efficient microbial systems for sustainable bioprocessing<ref>Li, T., Jiang, Q., Huang, J., Aitchison, C. M., Huang, F., Yang, M., Dykes, G. F., He, H. L., Wang, Q., Sprick, R. S., Cooper, A. I., & Liu, L. N. (2020). Reprogramming bacterial protein organelles as a nanoreactor for hydrogen production. Nature communications, 11(1), 5448. https://doi.org/10.1038/s41467-020-19280-0.</ref>. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
| + | In our experiment, we don't need to use the very original csoS operon. We choose to remove the csoS3 subunit from this operon. For more details about the part we eventually choose to adopt, please check [https://parts.igem.org/Part:BBa_K5115065 BBa_K5115065(cso, without csoS3)] | ||
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| + | ===Sequence and Features=== | ||
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<partinfo>BBa_K5115034 parameters</partinfo> | <partinfo>BBa_K5115034 parameters</partinfo> | ||
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| + | ==References== | ||
| + | <references /> | ||
Latest revision as of 10:15, 2 October 2024
csoS operon
Introduction
The csoS operon, originating from the Halothiobacillus neapolitanus, encodes a series of proteins essential for the assembly of α-carboxysomes, a type of microcompartment that facilitates the sequestration and concentration of enzymes involved in carbon fixation, particularly ribulose-1,5-bisphosphate carboxylase/oxygenase (Rubisco)[1]. In literature, α-carboxysomes have been extensively studied and successfully utilized in Escherichia coli for enhancing carbon fixation efficiency and optimizing metabolic pathways. The csoS operon includes key structural proteins including csoS4B, csoS1C, csoS1A, csoS1B, csoS1D, csoS4A, and CsoS2, which play crucial roles in forming the shell and encapsulating cargo enzymes, including those required for hydrogen production. The operon serves as a model for synthetic biology applications, particularly in constructing reactors capable of enhancing catalytic functions through encapsulation of heterologous enzymes. The successful expression of this operon in E. coli demonstrates its potential for industrial and biotechnological applications, enabling the creation of efficient microbial systems for sustainable bioprocessing[2].
Usage and Biology
In our experiment, we don't need to use the very original csoS operon. We choose to remove the csoS3 subunit from this operon. For more details about the part we eventually choose to adopt, please check BBa_K5115065(cso, without csoS3)
Sequence and Features
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NheI site found at 133
Illegal NotI site found at 6599 - 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 291
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 2805
Illegal AgeI site found at 799
Illegal AgeI site found at 1750
Illegal AgeI site found at 2431
Illegal AgeI site found at 4933 - 1000INCOMPATIBLE WITH RFC[1000]Illegal SapI site found at 191
References
- ↑ Oltrogge, L. M., Chaijarasphong, T., Chen, A. W., Bolin, E. R., Marqusee, S., & Savage, D. F. (2020). Multivalent interactions between CsoS2 and Rubisco mediate α-carboxysome formation. Nature structural & molecular biology, 27(3), 281–287. https://doi.org/10.1038/s41594-020-0387-7.
- ↑ Li, T., Jiang, Q., Huang, J., Aitchison, C. M., Huang, F., Yang, M., Dykes, G. F., He, H. L., Wang, Q., Sprick, R. S., Cooper, A. I., & Liu, L. N. (2020). Reprogramming bacterial protein organelles as a nanoreactor for hydrogen production. Nature communications, 11(1), 5448. https://doi.org/10.1038/s41467-020-19280-0.