Difference between revisions of "Part:BBa K5036008"

Latest revision as of 18:05, 13 September 2024

NES

Part Description

It is a Nuclear Export Signal which is a short sequence of amino acids found in certain proteins that direct those proteins out of the nucleus of a cell. . In our model it is engineered in the second chain of dCas9 synRTK receptor

Usage

It help in increasing control over transcription activity by preventing delivery of dCas9 into the nucleus without activation of our syn dCas9RTK receptor

this figure illustrates the structure of NES in the second chain of dCas9 synRTK receptor .

Literature Characterization

Many studies suggest that protein movement between the cell nucleus and cytoplasm (nucleocytoplasmic translocation) is controlled by signals called NLS and NES. While NLS is known to be essential for Mst3 protein entering the nucleus, it's unclear if there's also an NES signal directing full-length Mst3 back out to the cytoplasm. To investigate this possibility, HeLa cells were temporarily modified with a construct expressing EGFP-tagged Mst3 (EGFP-Mst3WT) and then treated with LMB, a drug that blocks a specific protein (Crm1) involved in exporting proteins from the nucleus.

The image reveals that EGFP-Mst3WT, normally found in the cytoplasm, concentrated in the nucleus following LMB treatment. This suggests the presence of a functional NES-like signal in Mst3. This signal might be responsible for exporting the full-length Mst3 protein from the nucleus through a mechanism dependent on the Crm1 protein.

Reference

Lee, W. S., Hsu, C. Y., Wang, P. L., Huang, C. Y. F., Chang, C. H., & Yuan, C. J. (2004). Identification and characterization of the nuclear import and export signals of the mammalian Ste20‐like protein kinase 3. FEBS letters, 572(1-3), 41-45.‏

Sequence and Features

Assembly Compatibility:

10
COMPATIBLE WITH RFC[10]
12
COMPATIBLE WITH RFC[12]
21
COMPATIBLE WITH RFC[21]
23
COMPATIBLE WITH RFC[23]
25
COMPATIBLE WITH RFC[25]
1000
COMPATIBLE WITH RFC[1000]

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 							"src="https://static.igem.wiki/teams/5036/parts/nes-attia.png">
 <p class=MsoNormal align=center style='text-align:left;border:none;width:98% ;justify-content:center;'><span
-lang=EN style='font-size:11.0pt;line-height:115%'>this figure illustrates the structure of NES in the second chain of syn dCas9RTK receptor
+lang=EN style='font-size:11.0pt;line-height:115%'>this figure illustrates the structure of NES in the second chain of dCas9 synRTK receptor
 . </span></p></div></html>
 ==Literature Characterization==
@@ Line 35: / Line 35: @@
 ">
 <p class=MsoNormal align=center style='text-align:left;border:none;width:98% ;justify-content:center;'><span
-lang=EN style='font-size:11.0pt;line-height:115%'>Figure A shows how the concentration of wild-type TEV protein compares to the L56V variant. A plateau in the absorption reading indicates the point at which the protein precipitates out of solution (limited solubility). Introducing mutations L56V and S135G significantly increased TEV solubility (Figure B), allowing them to reach maximum concentrations of 6.2 mg/mL and 5.77 mg/mL, respectively. Since the remaining variants (K45F, Q58F, E106G) displayed similar solubility to the wild-type TEV, they were not investigated further.
+lang=EN style='font-size:11.0pt;line-height:115%'>The image reveals that EGFP-Mst3WT, normally found in the cytoplasm, concentrated in the nucleus following LMB treatment. This suggests the presence of a functional NES-like signal in Mst3. This signal might be responsible for exporting the full-length Mst3 protein from the nucleus through a mechanism dependent on the Crm1 protein.
     </span></p></div></html>
+==Reference==
+Lee, W. S., Hsu, C. Y., Wang, P. L., Huang, C. Y. F., Chang, C. H., & Yuan, C. J. (2004). Identification and characterization of the nuclear import and export signals of the mammalian Ste20‐like protein kinase 3. FEBS letters, 572(1-3), 41-45.‏