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http://dx.doi.org/10.1007/s10059-009-0077-0

Differential Subcellular Localization of Ribosomal Protein L7 Paralogs in Saccharomyces cerevisiae  

Kim, Tae-Youl (School of Biological Sciences, and Research Center for Functional Cellulomics, Institute of Microbiology, Seoul National University)
Ha, Cheol Woong (School of Biological Sciences, and Research Center for Functional Cellulomics, Institute of Microbiology, Seoul National University)
Huh, Won-Ki (School of Biological Sciences, and Research Center for Functional Cellulomics, Institute of Microbiology, Seoul National University)
Abstract
In Saccharomyces cerevisiae, ribosomal protein L7, one of the ~46 ribosomal proteins of the 60S subunit, is encoded by paralogous RPL7A and RPL7B genes. The amino acid sequence identity between RPl7a and RPl7b is 97 percent; they differ by only 5 amino acid residues. Interestingly, despite the high sequence homology, Rpl7b is detected in both the cytoplasm and the nucleolus, whereas Rpl7a is detected exclusively in the cytoplasm. A site-directed mutagenesis experiment revealed that the change in the amino acid sequence of Rpl7b does not influence its subcellular localization. In addition, introns of RPL7A and RPL7B did not affect the subcellular localization of Rpl7a and Rpl7b. Remarkably, Rpl7b was detected exclusively in the cytoplasm in rpl7a knockout mutant, and overexpression of Rpl7a resulted in its accumulation in the nucleolus, indicating that the subcellular localization of Rpl7a and Rpl7b is influenced by the intracellular level of Rpl7a. Rpl7b showed a wide range of localization patterns, from exclusively cytoplasmic to exclusively nucleolar, in knockout mutants for some rRNA-processing factors, nuclear pore proteins, and large ribosomal subunit assembly factors. Rpl7a, however, was detected exclusively in the cytoplasm in these mutants. Taken together, these results suggest that although Rpl7a and Rpl7b are paralogous and functionally replaceable with each other, their precise physiological roles may not be identical.
Keywords
GFP; ribosomal protein L7; Saccharomyces cerevisiae; subcellular localization;
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1 Haarer, B., Viggiano, S., Hibbs, M.A., Troyanskaya, O.G., and Amberg, D.C. (2007). Modeling complex genetic interactions in a simple eukaryotic genome: actin displays a rich spectrum of complex haploinsufficiencies. Genes Dev. 21, 148-159   DOI   ScienceOn
2 Planta, R.J., and Mager, W.H. (1998). The list of cytoplasmic ribosomal proteins of Saccharomy cerevisiae. Yeast 14, 471-477   DOI   ScienceOn
3 Enyenihi, A.H., and Saunders, W.S. (2003). Large-scale functional genomic analysis of sporulation and meiosis in Saccharomyces cerevisiae. Genetics 163, 47-54   PUBMED
4 Ghaemmaghami, S., Huh, W.K., Bower, K., Howson, R.W., Belle, A., Dephoure, N., O'Shea, E.K., and Weissman, J.S. (2003). Global analysis of protein expression in yeast. Nature 425, 737-741   DOI   ScienceOn
5 Mizuta, K., Hashimoto, T., and Otaka, E. (1992). Yeast ribosomal proteins: XIII. Saccharomyces cerevisiae YL8A gene, interrupted with two introns, encodes a homolog of mammalian L7. Nucleic Acids Res. 20, 1011-1016   DOI   ScienceOn
6 Sherman, F. (2002). Getting started with yeast. Methods Enzymol. 350, 3-41   DOI   PUBMED
7 Gasch, A.P., Spellman, P.T., Kao, C.M., Carmel-Harel, O., Eisen, M.B., Storz, G., Botstein, D., and Brown, P.O. (2000). Genomic expression programs in the response of yeast cells to environmental changes. Mol. Biol. Cell 11, 4241-4257   DOI   PUBMED
8 Sikorski, R.S., and Hieter, P. (1989). A system of shuttle vectors and yeast host strains designed for efficient manipulation of DNA in Saccharomyces cerevisiae. Genetics 122, 19-27   PUBMED
9 Wach, A. (1996). PCR-synthesis of marker cassettes with long flanking homology regions for gene disruptions in S. cerevisiae. Yeast 12, 259-265   DOI   PUBMED   ScienceOn
10 Venema, J., and Tollervey, D. (1999). Ribosome synthesis in Saccharomyces cerevisiae. Annu. Rev. Genet. 33, 261-311   DOI   ScienceOn
11 Sung, M.K., Ha, C.W., and Huh, W.K. (2008). A vector system for efficient and economical switching of C-terminal epitope tags in Saccharomyces cerevisiae. Yeast 25, 301-311   DOI   ScienceOn
12 DeRisi, J.L., Iyer, V.R., and Brown, P.O. (1997). Exploring the metabolic and genetic control of gene expression on a genomic scale. Science 278, 680-686   DOI   PUBMED   ScienceOn
13 Ghazal, G., Ge, D., Gervais-Bird, J., Gagnon, J., and Abou Elela, S. (2005). Genome-wide prediction and analysis of yeast RNase III-dependent snoRNA processing signals. Mol. Cell. Biol. 25, 2981-2994   DOI   ScienceOn
14 Lohrum, M.A., Ludwig, R.L., Kubbutat, M.H., Hanlon, M., and Vousden, K.H. (2003). Regulation of HDM2 activity by the ribosomal protein L11. Cancer Cell 3, 577-587   DOI   ScienceOn
15 Dresios, J., Panopoulos, P., and Synetos, D. (2006). Eukaryotic ribosomal proteins lacking a eubacterial counterpart: important players in ribosomal function. Mol. Microbiol. 59, 1651-1663   DOI   ScienceOn
16 Lam, Y.W., Lamond, A.I., Mann, M., and Andersen, J.S. (2007). Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 17, 749-760   DOI   ScienceOn
17 Tate, W.P., and Poole, E.S. (2004). The ribosome: lifting the veil from a fascinating organelle. Bioessays 26, 582-588   DOI   ScienceOn
18 Enerly, E., Larsson, J., and Lambertsson, A. (2003). Silencing the Drosophila ribosomal protein L14 gene using targeted RNA interference causes distinct somatic anomalies. Gene 320, 41-48   DOI   PUBMED   ScienceOn
19 Amsterdam, A., Sadler, K.C., Lai, K., Farrington, S., Bronson, R.T., Lees, J.A., and Hopkins, N. (2004). Many ribosomal protein genes are cancer genes in zebrafish. PLoS Biol. 2, E139   DOI   PUBMED   ScienceOn
20 Huh, W.K., Falvo, J.V., Gerke, L.C., Carroll, A.S., Howson, R.W., Weissman, J.S., and O'Shea, E.K. (2003). Global analysis of protein localization in budding yeast. Nature 425, 686-691   DOI   ScienceOn
21 Sung, M.K., and Huh, W.K. (2007). Bimolecular fluorescence complementation analysis system for in vivo detection of proteinprotein interaction in Saccharomyces cerevisiae. Yeast 24, 767-775   DOI   ScienceOn
22 Lee, Y.L., and Lee, C.K. (2008). Transcriptional response according to strength of calorie restriction in Saccharomy cerevisiae. Mol. Cells 26, 299-307   PUBMED
23 Ni, L., and Snyder, M. (2001). A genomic study of the bipolar bud site selection pattern in Saccharomyces cerevisiae. Mol. Biol. Cell 12, 2147-2170   DOI   PUBMED
24 Rotenberg, M.O., Moritz, M., and Woolford, J.L. Jr. (1988). Depletion of Saccharomyces cerevisiae ribosomal protein L16 causes a decrease in 60S ribosomal subunits and formation of half-mer polyribosomes. Genes Dev. 2, 160-172   DOI   ScienceOn
25 Komili, S., Farny, N.G., Roth, F.P., and Silver, P.A. (2007). Functional specificity among ribosomal proteins regulates gene expression. Cell 131, 557-571   DOI   ScienceOn
26 Wool, I.G. (1996). Extraribosomal functions of ribosomal proteins. Trends Biochem. Sci. 21, 164-165   DOI   PUBMED
27 Degenhardt, R.F., and Bonham-Smith, P.C. (2008). Arabidopsis ribosomal proteins RPL23aA and RPL23aB are differentially targeted to the nucleolus and are desperately required for normal development. Plant Physiol. 147, 128-142   DOI   PUBMED   ScienceOn
28 Mazumder, B., Sampath, P., Seshadri, V., Maitra, R.K., DiCorleto, P.E., and Fox, P.L. (2003). Regulated release of L13a from the 60S ribosomal subunit as a mechanism of transcript-specific translational control. Cell 115, 187-198   DOI   ScienceOn
29 Mumberg, D., Muller, R., and Funk, M. (1995). Yeast vectors for the controlled expression of heterologous proteins in different ge netic backgrounds. Gene 156, 119-122   DOI   ScienceOn
30 Draptchinskaia, N., Gustavsson, P., Andersson, B., Pettersson, M., Willig, T.N., Dianzani, I., Ball, S., Tchernia, G., Klar, J., Matsson, H., et al. (1999). The gene encoding ribosomal protein S19 is mutated in Diamond-Blackfan anaemia. Nat. Genet 21, 169-175   DOI   ScienceOn