PMID: 9557704Apr 29, 1998Paper

Identification of a novel cellular TPR-containing protein, SGT, that interacts with the nonstructural protein NS1 of parvovirus H-1

Journal of Virology
C CziepluchJ C Jauniaux

Abstract

The nonstructural protein NS1 of autonomous parvoviruses is essential for viral DNA amplification and gene expression and is also the major cytopathic effector of these viruses. NS1 acts as nickase, helicase, and ATPase and upregulates P38-driven transcription of the capsid genes. We report here the identification of a novel cellular protein that interacts with NS1 from parvovirus H-1 and which we termed SGT, for small glutamine-rich tetratricopeptide repeat (TPR)-containing protein. The cDNA encoding full-length SGT was isolated through a two-hybrid screen with, as bait, the truncated NS1dlC69 polypeptide, which lacks the C-terminal transactivation domain of NS1. Full-length NS1 and SGT interacted in the two-hybrid system and in an in vitro interaction assay. Northern blot analysis revealed one major transcript of about 2 kb that was present in all rat tissues investigated. Rat sgt cDNA coded for 314 amino acids, and the protein migrated in sodium dodecyl sulfate-polyacrylamide gel electrophoresis with an apparent molecular mass of 34 kDa. SGT could be detected in both the nucleus and the cytoplasm of rat cells, as determined by indirect immunofluorescence analysis and Western blotting of fractionated cellular extracts with an...Continue Reading

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Citations

Apr 25, 2001·Biology of Reproduction·C J FlickingerJ C Herr
Apr 28, 2006·Journal of Virology·Jürg P F Nüesch, Jean Rommelaere
Jan 22, 2010·Stem Cell Reviews and Reports·Davood NasrabadiGhasem Hosseini Salekdeh
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Mar 25, 2021·Molecular Brain·Shun KubotaFumiaki Tanaka

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