Difference between revisions of "Part:BBa K1800002"

Revision as of 22:36, 14 October 2019

Horseradish Peroxidase

The Team TU Dresden 2019 used this biobrick to make the biobrick BBa_K3037007 adapted to the RFC 25 standard for making fusion proteins and use it to make the composite biobrick BBa_K3037003.

Class III plant peroxidases catalyze various oxidative reactions in which electrons are transferred to peroxide species, and substrate molecules are oxidized (Krainer, 2015). Peroxidases can be found in most plants and have been proposed to influence various functions related to the degradation of indole-3-acetic acid (IAA) (Lamport, 1986) and cell wall elasticity (Goldberg et al., 1986). Horseradish peroxidases is a peroxidase that has been used exhaustively as a reporter enzyme in diagnostics and histochemistry. In our lab, we designed an HRP part in accordance to RFC 10. HRP in our experiment will serve as a proof of concept for the Agrobacterium tumefaciens mediated transformation of tobacco plants with CBDA synthase. HRP will be inserted into the pORE vector for transformation of A. tumefaciens. The A. tumefaciens will then be used to transform tobacco plants. The tobacco will then produce hairy roots suspended in the culture that contains the HRP part.

References

Krainer, F. W., & Glieder, A. (2015). An updated view on horseradish peroxidases: recombinant production and biotechnological applications. Applied microbiology and biotechnology, 99(4), 1611-1625.

Lamport, D.T.A. 1986. Roles for peroxidase in cell wall genesis, p. 199-208. In: H. Greppin, C. Penel, and T. Gasper (eds.). Molecular and physiological aspects of plant peroxidase. Univ. of Geneva Press, Switzerland.

Lamport, D.T.A. 1986. Roles for peroxidase in cell wall genesis, p. 199-208. In: H. Greppin, C. Penel, and T. Gasper (eds.). Goldberg, R., A. Imberty, M. Liberman, and R. Prat. 1986. Relationships between peroxidase activities and cell wall plasticity, p. 209-220. In: H. Greppin, C. Penel, and T. Gasper (eds.). Molecular and physiological aspects of plant peroxidase. Univ. of Geneva Press, Switzerland.

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
INCOMPATIBLE WITH RFC[12]
Illegal NheI site found at 154
21
INCOMPATIBLE WITH RFC[21]
Illegal BglII site found at 396
Illegal XhoI site found at 480
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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-The Team TU Dresden 2019 used this biobrick to make the biobrick BBa_K3037007 adapted to the RFC 25 standard for making fusion proteins and use it to make the composite biobrick BBa_K3037003.
+The Team TU Dresden 2019 used this biobrick to make the biobrick [https://parts.igem.org/Part:BBa_K3037007 BBa_K3037007] adapted to the RFC 25 standard for making fusion proteins and use it to make the composite biobrick BBa_K3037003.
 Class III plant peroxidases catalyze various oxidative reactions in which electrons are transferred to peroxide species, and substrate molecules are oxidized (Krainer, 2015). Peroxidases can be found in most plants and have been proposed to influence various functions related to the degradation of indole-3-acetic acid (IAA) (Lamport, 1986) and cell wall elasticity (Goldberg et al., 1986). Horseradish peroxidases is a peroxidase that has been used exhaustively as a reporter enzyme in diagnostics and histochemistry. In our lab, we designed an HRP part in accordance to RFC 10. HRP in our experiment will serve as a proof of concept for the Agrobacterium <i>tumefaciens</i> mediated transformation of tobacco plants with CBDA synthase.  HRP will be inserted into the pORE vector for transformation of A. <i>tumefaciens</i>. The A. <i>tumefaciens</i> will then be used to transform tobacco plants. The tobacco will then produce hairy roots suspended in the culture that contains the HRP part.