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Sep 17, 2014
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Abstract

The Grg family of corepressor proteins lacks DNA-binding domain and these are recruited to the promoter region by interacting with DNA-binding transcription factors. Recruitment to the promoter by DNA-binding transcriptional factors results in transcriptional repression. There are five member of Grg proteins namely Grg1-5. Grg1-4 are the long forms and Grg5 is the short form of Grg family of corepressor. It has been reported that Grg proteins make tetramers to mediate the repression. In a collocatiozation assay, the full length myc-mGrg3 was transfected in COS7 cells along with mGrg5 and mGrg1∆280 fused with GFP. The colocalization assay indicates that full length myc-mGrg3 interacts with short form mGrg5-GFP by changing the localization pattern of mGrg5-GFP from cytoplasm to nucleus. In addition, we have also shown that Grg proteins interact with each other via N-terminal end, since myc-mGrg3 could not alter the translocation of non nuclear truncated form mGrg1∆280-GFP from cytoplasm into the nucleus. The inability of myc-mGrg3 to translocate mGrg1∆280-GFP indicates that Grg protein interact with each other only via N-terminal end. In conclusion, results we show here suggest that Grg protein interact with each other via N-terminal end and that this interaction alters the localization pattern of interacting Grg proteins.

Keywords: COS7 cells, Grg proteins, Colocalization assay.

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Author Biographies

Zulfiqar Ali Laghari, Sarfraz A Tunio, University of Sindh, jamshoro,

Department of Physiology,Department of Microbiology

 

Shaista Bano, Atif Patoli, Bushra Patoli, University of Sindh, jamshoro,

Department of Physiology,Department of Microbiology

How to Cite
Sarfraz A Tunio, Z. A. L., & Bushra Patoli, S. B. A. P. (2014). Protein-Protein Interaction Between the Short and Long Form of Grg Family of Co-Repressors. International Journal of Emerging Trends in Science and Technology, 1(07). Retrieved from https://igmpublication.org/ijetst.in/index.php/ijetst/article/view/340

References

1. Allen, T., M. van Tuyl, et al. (2006). "Grg1 acts as a lung-specific oncogene in a transgenic mouse model." Cancer Res 66(3): 1294-301.
2. Chen, G. and A. J. Courey (2000). "Groucho/TLE family proteins and transcriptional repression." Gene 249(1-2): 1-16.
3. Chen, G., P. H. Nguyen, et al. (1998). "A role for Groucho tetramerization in transcriptional repression." Mol Cell Biol 18(12): 7259-68.
4. Copley, R. R. (2005). "The EH1 motif in metazoan transcription factors." BMC Genomics 6: 169.
5. Formaz-Preston, A., J. R. Ryu, et al. (2012). "The Tbx20 homolog Midline represses wingless in conjunction with Groucho during the maintenance of segment polarity." Dev Biol 369(2): 319-29.
6. Imai, Y., M. Kurokawa, et al. (1998). "TLE, the human homolog of groucho, interacts with AML1 and acts as a repressor of AML1-induced transactivation." Biochem Biophys Res Commun 252(3): 582-9.
7. Li, S. S. (2000). "Structure and function of the Groucho gene family and encoded transcriptional corepressor proteins from human, mouse, rat, Xenopus, Drosophila and nematode." Proc Natl Sci Counc Repub China B 24(2): 47-55.
8. Nuthall, H. N., K. Joachim, et al. (2004). "Phosphorylation of serine 239 of Groucho/TLE1 by protein kinase CK2 is important for inhibition of neuronal differentiation." Mol Cell Biol 24(19): 8395-407.
9. Paroush, Z., R. L. Finley, Jr., et al. (1994). "Groucho is required for Drosophila neurogenesis, segmentation, and sex determination and interacts directly with hairy-related bHLH proteins." Cell 79(5): 805-15.
10. Patel, S. R., S. S. Bhumbra, et al. (2012). "Epigenetic mechanisms of Groucho/Grg/TLE mediated transcriptional repression." Mol Cell 45(2): 185-95.
11. Payankaulam, S. and D. N. Arnosti (2009). "Groucho corepressor functions as a cofactor for the Knirps short-range transcriptional repressor." Proc Natl Acad Sci U S A 106(41): 17314-9.
12. Pickles, L. M., S. M. Roe, et al. (2002). "Crystal structure of the C-terminal WD40 repeat domain of the human Groucho/TLE1 transcriptional corepressor." Structure 10(6): 751-61.
13. Pinto, M. and C. G. Lobe (1996). "Products of the grg (Groucho-related gene) family can dimerize through the amino-terminal Q domain." J Biol Chem 271(51): 33026-31.
14. Santisteban, P., P. Recacha, et al. (2010). "Dynamic expression of Groucho-related genes Grg1 and Grg3 in foregut endoderm and antagonism of differentiation." Dev Dyn 239(3): 980-6.
15. Sarma, N. J. and N. R. Yaseen (2011). "Amino-terminal enhancer of split (AES) interacts with the oncoprotein NUP98-HOXA9 and enhances its transforming ability." J Biol Chem 286(45): 38989-9001.
16. Sekiya, T. and K. S. Zaret (2007). "Repression by Groucho/TLE/Grg proteins: genomic site recruitment generates compacted chromatin in vitro and impairs activator binding in vivo." Mol Cell 28(2): 291-303.
17. Seo, W., H. Tanaka, et al. (2012). "Roles of VWRPY motif-mediated gene repression by Runx proteins during T-cell development." Immunol Cell Biol 90(8): 827-30.
18. Song, H., P. Hasson, et al. (2004). "Groucho oligomerization is required for repression in vivo." Mol Cell Biol 24(10): 4341-50.
19. Winkler, C. J., A. Ponce, et al. (2010). "Groucho-mediated repression may result from a histone deacetylase-dependent increase in nucleosome density." PLoS ONE 5(4): e10166.
20. Xia, H., M. Li, et al. (2013). "Suppression of RND3 activity by AES downregulation promotes cancer cell proliferation and invasion." Int J Mol Med 31(5): 1081-6.