Pom34 mRNA is the Only Target of the Sesa Network

Abstract

MPS2 is an essential gene required for the insertion of Saccharomyces cerevisiae centrosome into the nuclear membrane. Upon its deletion, cell cycle is stopped and the cell dies. Recently, we reported that SESA network can suppress essential role of MPS2. Detailed analysis showed that SESA is a system which suppresses centrosome duplication defects by inhibiting the translation of a subset of mRNAs selectively. In this study, we report the results of a genome-wide deletion screen which unearthed Pom34 mRNA as the only target of the SESA network.

Keywords

• S. cerevisiae,centrosome duplication,Pom34,SESA network

Pom34 mRNA’sı Sesa Ağının Tek Hedefidir

Abstract

S accharomyces cerevisiae sentrozomunun çekirdek zarına yerleşmesi için gerekli olan MPS2, bir elzem gendir. Bu genin silinmesi, hücre döngüsünü durdurur ve hücre ölümüne yol açar. Bir süre önce, SESA ağının MPS2 temel fonksiyonunu baskılayabildiğini gösterdik. Ayrıntılı analizler SESA sisteminin, maya sentrozomu eşlenmesi hatalarını gidermek için bir kısım mRNAnın translasyonunu seçici olarak baskıladığını ortaya koymuştur. Bu çalışmada ise genom ölçeğinde yaptığımız tarama ile Pom34 mRNAsının SESA ağnın tek hedefi olduğunu ortaya çıkardık

Keywords

• Saccharomyces cerevisiae,sentrozom eşlenmesi,Pom34,SESA ağı

References

1. 1. S.L. Jaspersen, M. Winey, The budding yeast spindle pole body: structure, duplication, and function, Annu. Rev. Cell Dev. Biol., 20 (2004) 1-28.
2. 2. M.A. D’Angelo, M.W. Hetzer, The role of the nuclear envelope in cellular organization, Cell. Mol. Life Sci., 63 (2006) 316–32.
3. 3. M. Winey, L. Goetsch, P. Baum, B. Byers, MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication, J. Cell Biol., 114 (1991) 745-54.
4. 4. M.C. Munoz-Centeno, S. McBratney, A. Monterrosa, B. Byers, C. Mann, M. Winey, Saccharomyces cerevisiae MPS2 encodes a membrane protein localized at the spindle pole body and the nuclear envelope, Mol. Biol. Cell, 10 (1999) 2393-406.
5. 5. B. Sezen, M. Seedorf, E. Schiebel, The SESA network links duplication of the yeast centrosome with the protein translation machinery, Genes Dev., 23 (2009) 1559-70.
6. 6. H.J. Chial, M.P. Rout, T.H. Giddings, M. Winey, Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies, J. Cell Biol., 143 (1998) 1789-1800.
7. 7. C.K. Lau, T.H.J. Giddings, M. Winey, A novel allele of Saccharomyces cerevisiae NDC1 reveals a potential role for the spindle pole body component Ndc1p in nuclear pore assembly, Eukaryot. Cell, 3 (2004) 447- 58.
8. 8. A.S. Madrid, J. Mancuso, W.Z. Cande, K. Weis, The role of the integral membrane nucleoporins Ndc1p and Pom152p in nuclear pore complex assembly and function, J. Cell Biol., 173 (2006) 361-71.

9. 9. J. Mansfeld, S. Guttinger, L.A. Hawryluk-Gara, N. Pante, M. Mall, V. Galy, U. Haselmann, P. Muhlhausser, R.W. Wozniak, I.W. Mattaj, U. Kutay, W. Antonin, The conserved transmembrane nucleoporin NDC1 is required for nuclear pore complex assembly in vertebrate cells, Mol. Cell, 22 (2006) 93-103.
10. 10. E. Onischenko, L.H. Stanton, A.S. Madrid, T. Kieselbach, K. Weis, Role of the Ndc1 interaction network in yeast nuclear pore complex assembly and maintenance, J. Cell Biol., 185 (2009) 475-91.
11. 11. P. Ross-Macdonald, P.S. Coelho, T. Roemer, S. Agarwal, A. Kumar, R. Jansen, K.H. Cheung, A. Sheehan, D. Symoniatis, L. Umansky, M. Heidtman, F.K. Nelson, H. Iwasaki, K. Hager, M. Gerstein, P. Miller, G.S. Roeder, M. Snyder, Large-scale analysis of the yeast genome by transposon tagging and gene disruption, Nature, 402 (1999) 413-18.
12. 12. C. Janke, M.M. Magiera, N. Rathfelder, C. Taxis, S. Reber, H. Maekawa, A. Moreno-Borchart, G. Doenges, E. Schwob, E. Schiebel, M. Knop, A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes, Yeast, 21 (2004) 947-62.
13. 13. S.S. Katta, J. Chen, J.M. Gardner, J.M. Friederichs, S.E. Smith, M. Gogol, J.R. Unruh, B.D. Slaughter, S.L. Jaspersen, Sec66-Dependent Regulation of Yeast Spindle-Pole Body Duplication Through Pom152, Genetics, 201 (2015) 1479-95.
14. 14. 14. B. Stebbins-Boaz, Q. Cao, C.H. de Moor, R. Mendez, J.D. Richter, Maskin is a CPEB-associated factor that transiently interacts with elF-4E, Mol. Cell, 4 (1999) 1017-27.
15. 15. N. Minshall, M.H. Reiter, D. Weil, N. Standart, CPEB interacts with an ovary-specific eIF4E and 4E-T in early Xenopus oocytes, J. Biol. Chem., 282 (2007) 37389-401.
16. 16. N. Standart, N. Minshall, Translational control in early development: CPEB, P-bodies and germinal granules, Biochem. Soc. Trans., 36 (2008) 671-6.
17. 17. A. Nakamura, K. Sato, K. Hanyu-Nakamura, Drosophila cup is an eIF4E binding protein that associates with Bruno and regulates oskar mRNA translation in oogenesis, Dev. Cell, 6 (2004) 69-78.
18. 18. M. Chekulaeva, M.W. Hentze, A. Ephrussi, Bruno acts as a dual repressor of oskar translation, promoting mRNA oligomerization and formation of silencing particles, Cell, 124 (2006) 521-33.
19. 19. J.D. Richter, N. Sonenberg, Regulation of capdependent translation by eIF4E inhibitory proteins, Nature, 433 (2005) 477-80.
20. 20. N. Sonenberg, A.G. Hinnebusch, Regulation of translation initiation in eukaryotes: mechanisms and biological targets, Cell, 136 (2009) 731-45.