Lens epithelium-derived growth factor/p75 interacts with the transposase-derived DDE domain of PogZ

Koen Bartholomeeusen, Frauke Christ, Jelle Hendrix, Jean-Christophe Rain, Stéphane Emiliani, Richard Benarous, Zeger Debyser, Rik Gijsbers, Jan De Rijck

Onderzoeksoutput: Bijdrage aan tijdschriftA2: Artikel in een internationaal wetenschappelijk tijdschrift met peer review, dat niet inbegrepen is in A1

Uittreksel

Lens epithelium-derived growth factor/p75 (LEDGF/p75) is a prominent cellular interaction partner of human immunodeficiency virus-1 (HIV-1) integrase, tethering the preintegration complex to the host chromosome. In light of the development of LEDGF/p75-integrase interaction inhibitors, it is essential to understand the cell biology of LEDGF/p75. We identified pogZ as new cellular interaction partner of LEDGF/p75. Analogous to lentiviral integrase, pogZ, a domesticated transposase, carries a DDE domain, the major determinant for LEDGF/p75 interaction. Using different in vitro and in vivo approaches, we corroborated the interaction between the C terminus of LEDGF/p75 and the DDE domain of pogZ, revealing an overlap in the binding of pogZ and HIV-1 integrase. Competition experiments showed that integrase is efficient in displacing pogZ from LEDGF/p75. Moreover, pogZ does not seem to play a role as a restriction factor of HIV. The finding that LEDGF/p75 is capable of interacting with a DDE domain protein that is not a lentiviral integrase points to a profound role of LEDGF/p75 in DDE domain protein function.

TaalEngels
TijdschriftJournal of Biological Chemistry
Volume284
Exemplaarnummer17
Pagina's (van-tot)11467-77
Aantal pagina's11
ISSN0021-9258
DOI's
StatusGepubliceerd - 24-apr-2009
Extern gepubliceerdJa

Trefwoorden

  • Amino Acid Sequence
  • Binding, Competitive
  • Cell Line, Tumor
  • HIV Integrase
  • HeLa Cells
  • Humans
  • Intercellular Signaling Peptides and Proteins
  • Lentivirus
  • Models, Biological
  • Molecular Sequence Data
  • Protein Structure, Tertiary
  • Recombinant Proteins
  • Sequence Homology, Amino Acid
  • Transposases
  • Two-Hybrid System Techniques

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