Difference between revisions of "Part:BBa K4765016"
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− | ''H. ex'' mtSSB is a type of mitochondrial single-stranded DNA binding protein derived from Hypsibius exemplaris . | + | ===Introduction=== |
+ | ''H. ex'' mtSSB is a type of mitochondrial single-stranded DNA binding protein derived from Hypsibius exemplaris . ''H. ex'' mtSSB is non-specific in binding single-stranded DNA. ssDNA is exposed by normal cellular functions like replication and transcription, as well as during genotoxic stress. DNA wrapped around H. ex mtSSB could be physically buffered against DNA damage and ensuing lethality. | ||
+ | Under harsh conditions like desiccation heat, and radiation, ''H. ex'' mtSSB can maintain the stability of DNA through the above mentioned mechanism, thus enhance the survival rate of organisms in harsh environments<ref>Hibshman, J. D., Clark-Hachtel, C. M., Bloom, K. S., & Goldstein, B. (2023). A bacterial expression cloning screen reveals tardigrade single-stranded DNA-binding proteins as potent desicco-protectants (2023.08.21.554171). bioRxiv. https://doi.org/10.1101/2023.08.21.554171</ref>. | ||
+ | ===Usage and Biology=== | ||
+ | We heterologously expressed ''H. ex'' mtSSB in ''E. coli'', conferring improved resistance to desiccation and UV radiation. We also compared its desiccation resistance with that of [https://parts.igem.org/Part:BBa_K2306003 Secretory-abundant heat soluble protein 33020 (SAHS 33020)] and tested the combined desiccation resistance of both proteins in [https://parts.igem.org/Part:BBa_K4765117 ribozyme+RBS+CDS+stem-loop module: ''H. ex'' mtSSB+SAHS 33020] | ||
+ | ===Characterization=== | ||
+ | |||
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+ | ==Reference== |
Revision as of 07:46, 1 October 2023
Hypsibius exemplaris mitochondrial single-stranded DNA binding protein (H. ex mtSSB)
Introduction
H. ex mtSSB is a type of mitochondrial single-stranded DNA binding protein derived from Hypsibius exemplaris . H. ex mtSSB is non-specific in binding single-stranded DNA. ssDNA is exposed by normal cellular functions like replication and transcription, as well as during genotoxic stress. DNA wrapped around H. ex mtSSB could be physically buffered against DNA damage and ensuing lethality. Under harsh conditions like desiccation heat, and radiation, H. ex mtSSB can maintain the stability of DNA through the above mentioned mechanism, thus enhance the survival rate of organisms in harsh environments[1].
Usage and Biology
We heterologously expressed H. ex mtSSB in E. coli, conferring improved resistance to desiccation and UV radiation. We also compared its desiccation resistance with that of Secretory-abundant heat soluble protein 33020 (SAHS 33020) and tested the combined desiccation resistance of both proteins in ribozyme+RBS+CDS+stem-loop module: H. ex mtSSB+SAHS 33020
Characterization
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25INCOMPATIBLE WITH RFC[25]Illegal NgoMIV site found at 186
- 1000INCOMPATIBLE WITH RFC[1000]Illegal BsaI.rc site found at 454
Illegal BsaI.rc site found at 535
Illegal SapI site found at 348
Reference
- ↑ Hibshman, J. D., Clark-Hachtel, C. M., Bloom, K. S., & Goldstein, B. (2023). A bacterial expression cloning screen reveals tardigrade single-stranded DNA-binding proteins as potent desicco-protectants (2023.08.21.554171). bioRxiv. https://doi.org/10.1101/2023.08.21.554171