Difference between revisions of "Part:BBa K3384315"
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Ste5ΔN-CTM is a highly active Ste5 mutant which can bind to the plasma membrane in the absence of pheromone. Ste5 is an important scaffold protein in the mating pheromone signaling pathway. The 214 amino acids at the N-terminus of Ste5 contain membrane binding sites and mediate the membrane localization of Ste5 under the control of Gβγ. By deleting the N-terminal sequence, the activation of Ste5 is independent of G protein. The C-terminal transmembrane domain of Snc2 was added to the Ste5ΔN C-terminus in order to constitutively recruit Ste5 to the plasma membrane1. As shown in figure 1, the Ste5ΔN-CTM protein can activate the MAPK pathway in the absence of pheromone and promote the expression of pheromone-responsive genes. | Ste5ΔN-CTM is a highly active Ste5 mutant which can bind to the plasma membrane in the absence of pheromone. Ste5 is an important scaffold protein in the mating pheromone signaling pathway. The 214 amino acids at the N-terminus of Ste5 contain membrane binding sites and mediate the membrane localization of Ste5 under the control of Gβγ. By deleting the N-terminal sequence, the activation of Ste5 is independent of G protein. The C-terminal transmembrane domain of Snc2 was added to the Ste5ΔN C-terminus in order to constitutively recruit Ste5 to the plasma membrane1. As shown in figure 1, the Ste5ΔN-CTM protein can activate the MAPK pathway in the absence of pheromone and promote the expression of pheromone-responsive genes. | ||
| − | [[File: NJTech China--Ste5ΔN-CTM1.png|width='100%' valign='top'| |center|thumb|550px|''<b>Fig.1</b> Structure and function of Ste5ΔN-CTM]] | + | [[File:T--NJTech China--Ste5ΔN-CTM1.png|width='100%' valign='top'| |center|thumb|550px|''<b>Fig.1</b> Structure and function of Ste5ΔN-CTM]] |
===Reference=== | ===Reference=== | ||
Revision as of 15:39, 26 October 2020
Ste5ΔN-CTM
Ste5ΔN-CTM is a highly active Ste5 mutant which can bind to the plasma membrane in the absence of pheromone. Ste5 is an important scaffold protein in the mating pheromone signaling pathway. The 214 amino acids at the N-terminus of Ste5 contain membrane binding sites and mediate the membrane localization of Ste5 under the control of Gβγ. By deleting the N-terminal sequence, the activation of Ste5 is independent of G protein. The C-terminal transmembrane domain of Snc2 was added to the Ste5ΔN C-terminus in order to constitutively recruit Ste5 to the plasma membrane1. As shown in figure 1, the Ste5ΔN-CTM protein can activate the MAPK pathway in the absence of pheromone and promote the expression of pheromone-responsive genes.
Reference
1. Lamson, R. E., Takahashi, S., Winters, M. J., and Pryciak, P. M. (2006) Dual role for membrane localization in yeast MAP kinase cascade activation and its contribution to signaling fidelity, Curr Biol 16, 618-623.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Illegal EcoRI site found at 365
Illegal SpeI site found at 1620
Illegal SpeI site found at 2166 - 12INCOMPATIBLE WITH RFC[12]Illegal EcoRI site found at 365
Illegal SpeI site found at 1620
Illegal SpeI site found at 2166 - 21INCOMPATIBLE WITH RFC[21]Illegal EcoRI site found at 365
Illegal BglII site found at 813
Illegal BglII site found at 2121
Illegal XhoI site found at 2058 - 23INCOMPATIBLE WITH RFC[23]Illegal EcoRI site found at 365
Illegal SpeI site found at 1620
Illegal SpeI site found at 2166 - 25INCOMPATIBLE WITH RFC[25]Illegal EcoRI site found at 365
Illegal SpeI site found at 1620
Illegal SpeI site found at 2166 - 1000COMPATIBLE WITH RFC[1000]