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Structure-Function Analysis of the Yeast Sumo Protease Ulp2

Structure-Function Analysis of the Yeast Sumo Protease Ulp2


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In the yeast Saccharomyces cerevisiae, two SUMO proteases, Ulp1 and Ulp2, are responsible for the cleavage of SUMO from a substrate protein, termed desumoylation. These two enzymes are active on a distinct subset of substrates, due to their different localization and enzymatic activities. Consequently, mutations in these two proteins cause differential growth defects and sensitivities to various stressors. There is limited homology between the two Ulps and it is restricted to their catalytically active Ulp domain (UD), a cysteine protease domain of about 200 amino acids. This study focuses on the non-catalytic domains of Ulp2 and the roles that each of these domains has in regulating its activity and localization. By phenotypic analysis of strains expressing Ulp2 derivatives lacking either the N- or C-terminal non-catalytic domain, I discovered that both non-catalytic domains of Ulp2 are required for full SUMO protease activity. The N-terminal non-catalytic domain, which contains multiple weak nuclear localization sequences, is required for nuclear localization and is essential for Ulp2 function in vivo. However, replacement of the entire Ulp2 N-terminal domain with an exogenous NLS restores the nuclear localization of Ulp2 and suppresses the evaluated defects of the ulp2Delta strain. There are two potential SUMO-interacting motifs (SIMs) in Ulp2. One is located in the C-terminal non-catalytic domain, while the second is close to the C-terminal end of the UD. Both SIMs are necessary for full Ulp2 function in vivo. A yeast two-hybrid assay revealed that the SIM in the C-terminal domain is indispensable for SUMO interaction, and in vitro binding studies indicate that the C-terminal fragment containing two SIMs contributes to the preference for polySUMO binding. In summary, these two distinct protein motifs are essential for full Ulp2 function. In mammalian cells, there are six distinct SUMO proteases (SENPs), two of which, SENP6 and SENP7, are closely related to Ulp2. Both SENP6 and SENP7 are the only SENPs to localize throughout the nucleus and to contain multiple SIMs. SENP6 is also active in desumoylating polySUMO chains. This characterization of yeast Ulp2 could therefore provide further insight into the functional specialization of mammalian SUMO proteases.


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Product Details
  • ISBN-13: 9781243645135
  • Publisher: Proquest, Umi Dissertation Publishing
  • Publisher Imprint: Proquest, Umi Dissertation Publishing
  • Height: 246 mm
  • Weight: 240 gr
  • ISBN-10: 124364513X
  • Publisher Date: 01 Sep 2011
  • Binding: Paperback
  • Spine Width: 7 mm
  • Width: 189 mm


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Structure-Function Analysis of the Yeast Sumo Protease Ulp2
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