Characterization of a Drosophila phosphorylation-dependent nuclear-localization-signal-binding protein

Imre Cserpán, Endre Máthé, A. Pátthy, A. Udvardy

Research output: Contribution to journalArticle

Abstract

A 94 kDa nuclear-localization-signal (NLS)-binding protein was purified from Drosophila embryos. The NLS of the simian-virus-40 T-antigen is Specifically bound by the dephosphorylated form of the protein. After phosphorylation, the affinity of the protein for the NLS is sharply decreased, In the dephosphorylated form, p94 (protein of 94 kDa) is the major NLS-binding protein in Drosophila embryos. Immunoprecipitation confirmed the ATP-dependent phosphorylation of p94, and co-precipitation of two additional phosphorylated proteins, indicated that the NLS-binding protein is part of a larger complex in Drosophila embryos. In agreement with the immunoprecipitation results, cross-linking experiments demonstrated the interaction of p94 with three additional proteins. These protein-protein interactions were also phosphorylation-dependent.

Original languageEnglish
Pages (from-to)821-826
Number of pages6
JournalBiochemical Journal
Volume328
Issue number3
Publication statusPublished - Dec 15 1997

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alpha Karyopherins
Phosphorylation
Drosophila
Proteins
Nuclear Localization Signals
Embryonic Structures
Immunoprecipitation
Viral Tumor Antigens
Simian virus 40
Coprecipitation
Nuclear Proteins
Viruses
Adenosine Triphosphate

ASJC Scopus subject areas

  • Biochemistry

Cite this

Characterization of a Drosophila phosphorylation-dependent nuclear-localization-signal-binding protein. / Cserpán, Imre; Máthé, Endre; Pátthy, A.; Udvardy, A.

In: Biochemical Journal, Vol. 328, No. 3, 15.12.1997, p. 821-826.

Research output: Contribution to journalArticle

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