Difference between revisions of "Part:BBa K4169006"
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<h3>References</h3> | <h3>References</h3> | ||
− | <p> | + | <p>[1] Yao J, Zhen X, Tang K, et al. Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system[J]. Nucleic acids research, 2020, 48(19): 11054-11067. |
+ | [2] Yao J, Guo Y, Zeng Z, et al. Identification and characterization of a HEPN‐MNT family type II toxin–antitoxin in S hewanella oneidensis[J]. Microbial biotechnology, 2015, 8(6): 961-973. | ||
+ | [3] Jia X, Yao J, Gao Z, et al. Structure–function analyses reveal the molecular architecture and neutralization mechanism of a bacterial HEPN–MNT toxin–antitoxin system[J]. Journal of Biological Chemistry, 2018, 293(18): 6812-6823.</p> |
Revision as of 17:05, 11 October 2022
HepT: a RNase like toxin
HepT is a toxin that can be effectively inhibited the growth of bacteria.The HepT toxin could function as an RNase with a RX4-6H active motif and cleave mRNA to inhibit cell growth. Complete with HepT (HZAU-China 2021:BBa_K3733010) was used in this study.
Usage and Biology
As an RNase enzyme, HepT can degrade mRNA at the transcriptional level, which ultimately leads to cell death
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal PstI site found at 103
Illegal PstI site found at 127 - 12INCOMPATIBLE WITH RFC[12]Illegal PstI site found at 103
Illegal PstI site found at 127 - 21COMPATIBLE WITH RFC[21]
- 23INCOMPATIBLE WITH RFC[23]Illegal PstI site found at 103
Illegal PstI site found at 127 - 25INCOMPATIBLE WITH RFC[25]Illegal PstI site found at 103
Illegal PstI site found at 127 - 1000COMPATIBLE WITH RFC[1000]
References
[1] Yao J, Zhen X, Tang K, et al. Novel polyadenylylation-dependent neutralization mechanism of the HEPN/MNT toxin/antitoxin system[J]. Nucleic acids research, 2020, 48(19): 11054-11067. [2] Yao J, Guo Y, Zeng Z, et al. Identification and characterization of a HEPN‐MNT family type II toxin–antitoxin in S hewanella oneidensis[J]. Microbial biotechnology, 2015, 8(6): 961-973. [3] Jia X, Yao J, Gao Z, et al. Structure–function analyses reveal the molecular architecture and neutralization mechanism of a bacterial HEPN–MNT toxin–antitoxin system[J]. Journal of Biological Chemistry, 2018, 293(18): 6812-6823.