Advanced search
Publication Cover
Bioscience, Biotechnology, and Biochemistry Volume 72, 2008 - Issue 7
Journal homepage
255
Views
14
CrossRef citations to date
0
Altmetric
Original Articles

SUMO Mediates Interaction of Ebp2p, the Yeast Homolog of Epstein-Barr Virus Nuclear Antigen 1-Binding Protein 2, with a RING Finger Protein Ris1p

Chiharu SHIRAIDepartment of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University
&
Keiko MIZUTADepartment of Biofunctional Science and Technology, Graduate School of Biosphere Science, Hiroshima University
Pages 1881-1886 | Received 03 Mar 2008, Accepted 16 Apr 2008, Published online: 22 May 2014

  • 1) Zhao, X., and Blobel, G., A SUMO ligase is part of a nuclear multiprotein complex that affects DNA repair and chromosomal organization. Proc. Natl. Acad. Sci. USA, 102, 4777–4782 (2005).
  • 2) Johnson, E. S., and Gupta, A. A., An E3-like factor that promotes SUMO conjugation to the yeast septins. Cell, 106, 735–744 (2001).
  • 3) Takahashi, Y., Kahyo, T., Toh-e, A., Yasuda, H., and Kikuchi, Y., Yeast Ull1/Siz1 is a novel SUMO1/Smt3 ligase for septin components and functions as an adaptor between conjugating enzyme and substrates. J. Biol. Chem., 276, 48973–48977 (2001).
  • 4) Tsujii, R., Miyoshi, K., Tsuno, A., Matsui, Y., Toh-e, A., Miyakawa, T., and Mizuta, K., Ebp2p, yeast homologue of a human protein that interacts with Epstein-Barr virus Nuclear Antigen 1, is required for pre-rRNA processing and ribosomal subunit assembly. Genes Cells, 5, 543–553 (2000).
  • 5) Shirai, C., Takai, T., Nariai, M., Horigome, C., and Mizuta, K., Ebp2p, the yeast homolog of Epstein-Barr virus nuclear antigen 1-binding protein 2, interacts with factors of both the 60 S and the 40 S ribosomal subunit assembly. J. Biol. Chem., 279, 25353–25358 (2004).
  • 6) Bachant, J., Alcasabas, A., Blat, Y., Kleckner, N., and Ellege, S. J., The SUMO-1 isopeptidase Smt4 is linked to centromeric cohesion through SUMO-1 modification of DNA topoisomerase II. Mol. Cell, 9, 1169–1182 (2002).
  • 7) James, P., Halladay, J., and Craig, E. A., Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast. Genetics, 144, 1425–1436 (1996).
  • 8) Hollenberg, S. M., Sternglanz, R., Cheng, P. F., and Weintraub, H., Identification of a new family of tissue-specific basic helix-loop-helix proteins with a two-hybrid system. Mol. Cell. Biol., 15, 3813–3822 (1995).
  • 9) Miller, J. H., “Experiments in Molecular Genetics,” Cold Spring Harbor Laboratory Press, Cold Spring Harbor, pp. 352–355 (1972).
  • 10) Pringle, J. R., Adams, A. E. M., Drubin, D. G., and Haarer, B. K., Immunofluorescence methods for yeast. Methods Enzymol., 194, 565–602 (1991).
  • 11) Tsuno, A., Miyoshi, K., Tsujii, R., Miyakawa, T., and Mizuta, K., RRS1, a conserved essential gene, encodes a novel regulatory protein required for ribosome biogenesis in Saccharomyces cerevisiae. Mol. Cell. Biol., 20, 2066–2074 (2000).
  • 12) Nariai, M., Tanaka, T., Okada, T., Shirai, C., Horigome, C., and Mizuta, K., Synergistic defect in 60S ribosomal subunit assembly caused by a mutation of Rrs1p, a ribosomal protein L11-binding protein, and 3′-extension of 5S rRNA in Saccharomyces cerevisiae. Nucleic Acids Res., 33, 4553–4562 (2005).
  • 13) Takahashi, Y., Toh-e, A., and Kikuchi, Y., Comparative analysis of yeast PIAS-type SUMO ligase in vivo and in vitro. J. Biochem., 133, 415–422 (2003).
  • 14) Stead, K., Aguilar, C., Hartman, T., Drexel, M., Meluh, P., and Guacci, V., Pds5p regulates the maintenance of sister chromatid cohesion and is sumoylated to promote the dissolution of cohesion. J. Cell Biol., 163, 729–741 (2003).
  • 15) Hochstrasser, M., SP-RING for SUMO: new functions bloom for a ubiquitin-like protein. Cell, 107, 5–8 (2001).
  • 16) Song, J., Durrin, L. K., Wilkinson, T. A., Krontiris, T. G., and Chen, Y., Identification of a SUMO-binding motif that recognizes SUMO-modified proteins. Proc. Natl. Acad. Sci. USA, 101, 14373–14378 (2004).
  • 17) Hannich, J. T., Lewis, A., Kroetz, M. B., Li, S. J., Heide, H., Emili, A., and Hochstrasser, M., Defining the SUMO-modified proteome by multiple approaches in Saccharomyces cerevisiae. J. Biol. Chem., 280, 4102–4110 (2005).
  • 18) Zhang, Z., and Buchman, A. R., Identification of a member of a DNA-dependent ATPase family that causes interference with silencing. Mol. Cell. Biol., 17, 5461–5472 (1997).
  • 19) Biggins, S., Bhalla, N., Chang, A., Smith, D. L., and Murray, A. W., Genes involved in sister chromatid separation and segregation in the budding yeast Saccharomyces cerevisiae. Genetics, 159, 453–470 (2001).
  • 20) O’Neill, B. M., Hanway, D., Winzeler, E. A., and Romesberg, F. E., Coordinated functions of WSS1, PSY2 and TOF1 in the DNA damage response. Nucleic Acids Res., 32, 6519–6530 (2004).
  • 21) Johnson, E. S., and Blobel, G., Cell cycle-regulated attachment of the ubiquitin-related protein SUMO to the yeast septins. J. Cell Biol., 147, 981–994 (1999).
  • 22) Iwase, M., and Toh-e, A., Nis1 encoded by YNL078W: a new neck protein of Saccharomyces cerevisiae. Genes Genet. Syst., 76, 335–343 (2001).
  • 23) Denison, C., Rudner, A. D., Gerber, S. A., Bakalarski, C. E., Moazed, D., and Gygi, S. P., A proteomic strategy for gaining insights into protein sumoylation in yeast. Mol. Cell. Proteomics, 4, 246–254 (2004).
  • 24) Panse, V. G., Hardeland, U., Werner, T., Kuster, B., and Hurt, E., A proteome-wide approach identifies sumoylated substrate proteins in yeast. J. Biol. Chem., 279, 41346–41351 (2004).
  • 25) Wohlschlegel, J. A., Johnson, E. S., Reed, S. I., and Yates, J. R., III, Global analysis of protein sumoylation in Saccharomyces cerevisiae. J. Biol. Chem., 279, 45662–45668 (2004).
  • 26) Wykoff, D. D., and O’Shea, E. K., Identification of sumoylated proteins by systematic immunoprecipitation of the budding yeast proteome. Mol. Cell. Proteomics, 4, 73–83 (2005).
  • 27) Zhou, W., Ryan, J. J., and Zhou, H., Global analyses of sumoylated proteins in Saccharomyces cerevisiae: induction of protein sumoylation by cellular stresses. J. Biol. Chem., 279, 32262–32268 (2004).
  • 28) Schwienhorst, I., Johnson, E. S., and Dohmen, R. J., SUMO conjugation and deconjugation. Mol. Gen. Genet., 263, 771–786 (2000).
  • 29) Seeler, J. S., and Dejean, A., Nuclear and unclear functions of SUMO. Nat. Rev. Mol. Cell Biol., 4, 690–699 (2003).
  • 30) Uzunova, K., Göttsche, K., Miteva, M., Weisshaar, S. R., Glanemann, C., Schnellhardt, M., Niessen, M., Scheel, H., Hofmann, K., Johnson, E. S., Praefcke, G. J. K., and Dohmen, R. J., Ubiquitin-dependent proteolytic control of SUMO conjugates. J. Biol. Chem., 282, 34167–34175 (2007).

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Order Reprints Request Corporate Permissions

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

Request Academic Permissions

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.

Related research

People also read lists articles that other readers of this article have read.

Recommended articles lists articles that we recommend and is powered by our AI driven recommendation engine.

Cited by lists all citing articles based on Crossref citations.
Articles with the Crossref icon will open in a new tab.