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Updated: Sep 27, 2026

Localization of SUMO-modified Proteins Using Fluorescent Sumo-trapping Proteins
Published on: April 27, 2019
Non-covalent interaction between nucleocapsid protein of Tula hantavirus and small ubiquitin-related modifier-1,
Pasi Kaukinen1, Antti Vaheri, Alexander Plyusnin
1Department of Virology, Haartman Institute, PO Box 21, University of Helsinki, FIN-00014, Helsinki, Finland. psi.kaukinen@helsinki.fi
Abstract:
To find cellular binding counterparts for the nucleocapsid protein (N) of Tula hantavirus (TULV), two cDNA libraries were screened using yeast two-hybrid systems based on LexA and Gal4 transcription factors. Five cDNA clones encoding SUMO-1 (Small Ubiquitin-related MOdifier, also known as sentrin) were selected in the LexA system. Confocal microscopy revealed that, in infected cells, TULV N protein and SUMO-1 colocalize at the perinuclear area providing further evidence for interaction between the two proteins. Neither endogenous nor transiently expressed SUMO-1 was found to be covalently linked to the N protein. Additional evidence that the interaction is non-covalent was obtained in immunoprecipitation experiments: N protein-specific antibodies precipitated SUMO-1 from TULV-infected Vero E6 cell lysate. By using a pepscan assay, two basic amino acid stretches in the N-terminal part of SUMO-1 were shown to be involved in the interaction.
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