Acta Biologica Hungarica

, Volume 62, Issue 4, pp 397–412 | Cite as

In vivo effects of abolishing the Single canonical sumoylation site in the C-terminal region of Drosophila p53

  • N. Pardi
  • Edith Vámos
  • Zsuzsanna Ujfaludi
  • O. Komonyi
  • L. Bodai
  • I. M. BorosEmail author


Using yeast two-hybrid screens we determined that Drosophila (Dm)p53 interacts with proteins involved in sumoylation (UBA2, UBC9 and PIAS) through different regions of its C-terminal domain. A K302R point mutation within a single canonical sumoylation site of Dmp53 did not abolish the observed interactions. These observations prompted us to analyze whether Dmp53 sumoylation at this site has any functional role in vivo. Genetic assays showed that deleting one copy of genes involved in sumoylation (lwr, Su(var)2–10 or smt3 heterozygosity) enhanced slightly the mutator phenotype of Dmp53. We compared the in vivo effects of wild type and K302R Dmp53 overproduced from transgenes and determined that similar levels of expression of the mutant and wild type proteins resulted in similar phenotype, and the two proteins showed similar cellular localization. The half life and the trans-activator activity of K302R mutant and wild type Dmp53 were also comparable. Lastly, by analyzing wild type and K302R Dmp53 expressed at different levels in animals and in S2 cells we detected no differences between the mobility of the mutant and wild-type protein. From these data we conclude that under normal developmental conditions the loss of SUMO modification at K302 does not affect Dmp53 function significantly.


p53 SUMO apoptosis Drosophila yeast two hybrid 



Basic Local Alignment Search Tool


fluorescence activated cell sorting


gluthation S-transferase


multiple wing hair


Trp-, Ura-, Leu-, Lys-, His-


yeast two-hybrid


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© Akadémiai Kiadó, Budapest 2011

This article is distributed under the terms of the Creative Commons Attribution 4.0 International License (, which permits unrestricted use, distribution, and reproduction in any medium, provided you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made.

Authors and Affiliations

  • N. Pardi
    • 1
  • Edith Vámos
    • 1
  • Zsuzsanna Ujfaludi
    • 2
  • O. Komonyi
    • 2
  • L. Bodai
    • 2
  • I. M. Boros
    • 1
    • 2
    Email author
  1. 1.Institute of BiochemistryBiological Research CenterSzegedHungary
  2. 2.Chromatin Research Group of HAS, Department of Biochemistry and Molecular BiologyUniversity of SzegedSzegedHungary

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