Araştırma Makalesi
Yıl 2018,
Sayı: 4, 82 - 86, 04.12.2018
Öz
The
correct separation of chromosomes during mitosis is necessary to prevent
genetic instability and aneuploidy which causes cancer, and other diseases. The
main criteria for this is the correct duplication of the centrosome. Recently,
we reported that Smy2 can suppress the essential role of MPS2 in the insertion of yeast centrosome into the nuclear membrane
and co-operates with Eap1, Scp160, Asc1 for this task. We gave the name SESA (Smy2,
Eap1, Scp160, Asc1) network to the system consisting of
these four proteins. Detailed analysis showed that the SESA system is part of a
mechanism which regulates translation of POM34
mRNA. Thus, SESA, is a system which suppresses spindle pole body (SPB)
duplication defects by inhibiting the translation of POM34 mRNA (Sezen,
et al., 2009). Although many important points regarding SESA network
have been discovered, many others remain obscure. In this study, we performed a
genome-wide screen in order to unearth new members of the system and showed
that Dhh1 is a member of the SESA network. Dhh1 is a known cytoplasmic DEAD-box
helicase known to play role in translational regulation. Thus we propose that
Dhh1 contributes to the highly selective nature of the inhibition of translation
by SESA system.
Anahtar Kelimeler
S. cerevisiae Centrosome duplication Translational control SESA network
Kaynakça
- Adams, I. R., Kilmartin, J. V. (1999). Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae. Journal of Cell Biology, 145,809–823. Araki, Y., Lau, C. K., Maekawa, H., Jaspersen, S. L., Giddings, J. T. H., Schiebel, E., Winey, M. (2006). The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is required for SPB membrane insertion and interacts with the integral membrane proteins Ndc1p and Mps2p. Molecular Biology of the Cell, 17,1959–1970. Ash, M. R., Faelber, K., Kosslick, D., Albert, G. L., Roske, Y., Kofler, M., Schuemann, M., Krause, E., Freund, C. (2010). Conserved β-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes. Structure, 18,944–954. Baum, S., Bittins, M., Frey, S., Seedorf, M. (2004). Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes. Biochemistry Journal, 380,823-830. Blewett, N. H., Goldstrohm, A. C. (2012). A eukaryotic translation initiation factor 4E-binding protein promotes mRNA decapping and is required for PUF repression. Molecular and Cellular Biology, 32,4181-4194. Bullit, E., Rout, M. P., Kilmartin, J. V., Akey C. W. (1997). The yeast spindle pole body is assembled around a central crystal of Spc42p. Cell, 89,1077–1086. Carroll, J. S., Munchel, S. E., Weis, K. (2011). The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics. Journal of Cell Biology, 194,527-537. Chial, H. J., Rout, M. P., Giddings, T. H., Winey, M. (1998). Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. Journal of Cell Biology, 143,1789–1800. Elliott, S., Knop, M., Schlenstedt, G., Schiebel, E. (1999). Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proceeding of the National Academy of Science USA, 96,6205–6210. Ergüden, B. (2017). Pom34 mRNA is the Only Target of the SESA Network. Hacettepe Journal of Biology and Chemistry, 45,539-545. Georgiev, A., Sjostrom, M., Wieslander, A. (2007). Binding specificities of the GYF domains from two Saccharomyces cerevisiae paralogs. Protein Engineering and Design Sel, 20,443-52. Higashio, H., Sato, K., Nakano, A. (2008). Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex. Traffic, 9,79-93. Jackson, C. L., Kepes, F. (1994). BFR1, a multicopy suppressor of brefeldin A-induced lethality, is implicated in secretion and nuclear segregation in Saccharomyces cerevisiae. Genetics, 137, 423-437. Janke, C., Magiera, M. M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A., Doenges, G., Schwob, E., Schiebel, E., Knop, M. (2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast, 21,947-962. Jaspersen, S. L., Giddings, T. H. Jr., Winey, M. (2002). Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. Journal of Cell Biology, 159,945–956. Jaspersen, S. L., Winey, M. (2004). The budding yeast spindle pole body: structure, duplication, and function. Annual Reviews of Cellular and Developmental Biology, 20,1–28. Kofler, M., Motzny, K., Freund C. (2005). GYF domain proteomics reveals interaction sites in known and novel target proteins. Molecular and Cellular Proteomics, 4,1797-1811. Lang, B. D., Li, A., Black-Brewster, H. D., Fridovich-Keil J. L. (2001). The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Nucleic Acids Research, 29,2567-2574. Li, A. M., Watson, A., Fridovich-Keil, J. L. (2003). Scp160p associates with specific mRNAs in yeast. Nucleic Acids Research, 31,1830-1837. Li, A. M., Watson, A., Fridovich-Keil, J. L. (2004). Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Nucleic Acids Research, 32, 4768-4775. Miao, M., Ryan, K. J., Wente, S. R. (2006). The integral membrane protein Pom34p functionally links nucleoporin subcomplexes. Genetics, 172,1441-1457. Mitchell, S. F., Jain, S., She, M., Parker, R. (2012). Global analysis of yeast mRNPs. Nature Structural Molecular Biology, 20,127-133. Munoz-Centeno, M. C., McBratney, S., Monterrosa, A., Byers, B., Mann, C., Winey, M. (1999). Saccharomyces cerevisiae MPS2 encodes a membrane protein localized at the spindle pole body and the nuclear envelope. Molecular Biology of the Cell, 10,2393-2406. Nakamura, A., Amikura, R., Hanyu, K., Kobayashi, S. (2001). Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex during Drosophila oogenesis. Development, 128, 3233-3242. Nishikawa, S., Terazawa, Y., Nakayama, T., Hirata, A., Makio, T. (2003). Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion. J Biol Chem, 278,9938–9943. Rose, M. D., Fink, G. R. (1987). KAR1, a gene required for function of both intranuclear and extranuclear microtubules in yeast. Cell, 48,1047–1060. Ross-Macdonald, P., Coelho, P. S., Roemer, T., Agarwal, S., Kumar, A., Jansen, R., Cheung, K. H., Sheehan, A., Symoniatis, D., Umansky, .L, Heidtman, M., Nelson, F. K., Iwasaki, H., Hager, K., Gerstein, M., Miller, P., Roeder, G. S., Snyder, M. (1999). Large-scale analysis of the yeast genome by transposon tagging and gene disruption. Nature, 402,413-418. Schramm, C., Elliott, S., Shevchenko, A., Schiebel, E. (2000). The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is essential for SPB duplication. EMBO Journal, 19,421–433. Sezen (Ergüden), B., Seedorf, M., Schiebel, E. (2009). The SESA network links duplication of the yeast centrosome with the protein translation machinery. Genes & Development, 23, 1559–1570. Sezen (Ergüden), B. (2015). Reduction of Saccharomyces cerevisiae Pom34 protein level by SESA network is related to membrane lipid composition. FEMS Yeast Research,15,fov089. Smillie, D. A., Sommerville, J. (2002). RNA helicase p54 (DDX6) is a shuttling protein involved in nuclear assembly of stored mRNP particles. Journal of Cell Science, 115, 395-407. Spang, A., Courtney, I., Grein, K., Matzner, M., Schiebel, E. (1995). The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body. Journal of Cell Biology, 128,863–877. Winey, M., Goetsch, L., Baum, P., Byers, B. (1991). MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication. Journal of Cell Biology, 114,745–754. Winey, M., Hoyt, M. A., Chan, C., Goetsch, L., Botstein, D. (1993). NDC1: a nuclear periphery component required for yeast spindle pole body duplication. Journal of Cell Biology, 122,743–751.
Yıl 2018,
Sayı: 4, 82 - 86, 04.12.2018
Öz
Kaynakça
- Adams, I. R., Kilmartin, J. V. (1999). Localization of core spindle pole body (SPB) components during SPB duplication in Saccharomyces cerevisiae. Journal of Cell Biology, 145,809–823. Araki, Y., Lau, C. K., Maekawa, H., Jaspersen, S. L., Giddings, J. T. H., Schiebel, E., Winey, M. (2006). The Saccharomyces cerevisiae spindle pole body (SPB) component Nbp1p is required for SPB membrane insertion and interacts with the integral membrane proteins Ndc1p and Mps2p. Molecular Biology of the Cell, 17,1959–1970. Ash, M. R., Faelber, K., Kosslick, D., Albert, G. L., Roske, Y., Kofler, M., Schuemann, M., Krause, E., Freund, C. (2010). Conserved β-hairpin recognition by the GYF domains of Smy2 and GIGYF2 in mRNA surveillance and vesicular transport complexes. Structure, 18,944–954. Baum, S., Bittins, M., Frey, S., Seedorf, M. (2004). Asc1p, a WD40-domain containing adaptor protein, is required for the interaction of the RNA-binding protein Scp160p with polysomes. Biochemistry Journal, 380,823-830. Blewett, N. H., Goldstrohm, A. C. (2012). A eukaryotic translation initiation factor 4E-binding protein promotes mRNA decapping and is required for PUF repression. Molecular and Cellular Biology, 32,4181-4194. Bullit, E., Rout, M. P., Kilmartin, J. V., Akey C. W. (1997). The yeast spindle pole body is assembled around a central crystal of Spc42p. Cell, 89,1077–1086. Carroll, J. S., Munchel, S. E., Weis, K. (2011). The DExD/H box ATPase Dhh1 functions in translational repression, mRNA decay, and processing body dynamics. Journal of Cell Biology, 194,527-537. Chial, H. J., Rout, M. P., Giddings, T. H., Winey, M. (1998). Saccharomyces cerevisiae Ndc1p is a shared component of nuclear pore complexes and spindle pole bodies. Journal of Cell Biology, 143,1789–1800. Elliott, S., Knop, M., Schlenstedt, G., Schiebel, E. (1999). Spc29p is a component of the Spc110p subcomplex and is essential for spindle pole body duplication. Proceeding of the National Academy of Science USA, 96,6205–6210. Ergüden, B. (2017). Pom34 mRNA is the Only Target of the SESA Network. Hacettepe Journal of Biology and Chemistry, 45,539-545. Georgiev, A., Sjostrom, M., Wieslander, A. (2007). Binding specificities of the GYF domains from two Saccharomyces cerevisiae paralogs. Protein Engineering and Design Sel, 20,443-52. Higashio, H., Sato, K., Nakano, A. (2008). Smy2p participates in COPII vesicle formation through the interaction with Sec23p/Sec24p subcomplex. Traffic, 9,79-93. Jackson, C. L., Kepes, F. (1994). BFR1, a multicopy suppressor of brefeldin A-induced lethality, is implicated in secretion and nuclear segregation in Saccharomyces cerevisiae. Genetics, 137, 423-437. Janke, C., Magiera, M. M., Rathfelder, N., Taxis, C., Reber, S., Maekawa, H., Moreno-Borchart, A., Doenges, G., Schwob, E., Schiebel, E., Knop, M. (2004). A versatile toolbox for PCR-based tagging of yeast genes: new fluorescent proteins, more markers and promoter substitution cassettes. Yeast, 21,947-962. Jaspersen, S. L., Giddings, T. H. Jr., Winey, M. (2002). Mps3p is a novel component of the yeast spindle pole body that interacts with the yeast centrin homologue Cdc31p. Journal of Cell Biology, 159,945–956. Jaspersen, S. L., Winey, M. (2004). The budding yeast spindle pole body: structure, duplication, and function. Annual Reviews of Cellular and Developmental Biology, 20,1–28. Kofler, M., Motzny, K., Freund C. (2005). GYF domain proteomics reveals interaction sites in known and novel target proteins. Molecular and Cellular Proteomics, 4,1797-1811. Lang, B. D., Li, A., Black-Brewster, H. D., Fridovich-Keil J. L. (2001). The brefeldin A resistance protein Bfr1p is a component of polyribosome-associated mRNP complexes in yeast. Nucleic Acids Research, 29,2567-2574. Li, A. M., Watson, A., Fridovich-Keil, J. L. (2003). Scp160p associates with specific mRNAs in yeast. Nucleic Acids Research, 31,1830-1837. Li, A. M., Watson, A., Fridovich-Keil, J. L. (2004). Both KH and non-KH domain sequences are required for polyribosome association of Scp160p in yeast. Nucleic Acids Research, 32, 4768-4775. Miao, M., Ryan, K. J., Wente, S. R. (2006). The integral membrane protein Pom34p functionally links nucleoporin subcomplexes. Genetics, 172,1441-1457. Mitchell, S. F., Jain, S., She, M., Parker, R. (2012). Global analysis of yeast mRNPs. Nature Structural Molecular Biology, 20,127-133. Munoz-Centeno, M. C., McBratney, S., Monterrosa, A., Byers, B., Mann, C., Winey, M. (1999). Saccharomyces cerevisiae MPS2 encodes a membrane protein localized at the spindle pole body and the nuclear envelope. Molecular Biology of the Cell, 10,2393-2406. Nakamura, A., Amikura, R., Hanyu, K., Kobayashi, S. (2001). Me31B silences translation of oocyte-localizing RNAs through the formation of cytoplasmic RNP complex during Drosophila oogenesis. Development, 128, 3233-3242. Nishikawa, S., Terazawa, Y., Nakayama, T., Hirata, A., Makio, T. (2003). Nep98p is a component of the yeast spindle pole body and essential for nuclear division and fusion. J Biol Chem, 278,9938–9943. Rose, M. D., Fink, G. R. (1987). KAR1, a gene required for function of both intranuclear and extranuclear microtubules in yeast. Cell, 48,1047–1060. Ross-Macdonald, P., Coelho, P. S., Roemer, T., Agarwal, S., Kumar, A., Jansen, R., Cheung, K. H., Sheehan, A., Symoniatis, D., Umansky, .L, Heidtman, M., Nelson, F. K., Iwasaki, H., Hager, K., Gerstein, M., Miller, P., Roeder, G. S., Snyder, M. (1999). Large-scale analysis of the yeast genome by transposon tagging and gene disruption. Nature, 402,413-418. Schramm, C., Elliott, S., Shevchenko, A., Schiebel, E. (2000). The Bbp1p-Mps2p complex connects the SPB to the nuclear envelope and is essential for SPB duplication. EMBO Journal, 19,421–433. Sezen (Ergüden), B., Seedorf, M., Schiebel, E. (2009). The SESA network links duplication of the yeast centrosome with the protein translation machinery. Genes & Development, 23, 1559–1570. Sezen (Ergüden), B. (2015). Reduction of Saccharomyces cerevisiae Pom34 protein level by SESA network is related to membrane lipid composition. FEMS Yeast Research,15,fov089. Smillie, D. A., Sommerville, J. (2002). RNA helicase p54 (DDX6) is a shuttling protein involved in nuclear assembly of stored mRNP particles. Journal of Cell Science, 115, 395-407. Spang, A., Courtney, I., Grein, K., Matzner, M., Schiebel, E. (1995). The Cdc31p-binding protein Kar1p is a component of the half bridge of the yeast spindle pole body. Journal of Cell Biology, 128,863–877. Winey, M., Goetsch, L., Baum, P., Byers, B. (1991). MPS1 and MPS2: novel yeast genes defining distinct steps of spindle pole body duplication. Journal of Cell Biology, 114,745–754. Winey, M., Hoyt, M. A., Chan, C., Goetsch, L., Botstein, D. (1993). NDC1: a nuclear periphery component required for yeast spindle pole body duplication. Journal of Cell Biology, 122,743–751.
Toplam 1 adet kaynakça vardır.
Ayrıntılar
| Birincil Dil | İngilizce |
|---|---|
| Konular | Mühendislik |
| Bölüm | Makaleler |
| Yazarlar | |
| Yayımlanma Tarihi | 4 Aralık 2018 |
| Yayımlandığı Sayı | Yıl 2018 Sayı: 4 |
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