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The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells.
Ogilvie, V C; Wilson, B J; Nicol, S M; Morrice, N A; Saunders, L R; Barber, G N; Fuller-Pace, F V.
Afiliación
  • Ogilvie VC; Department of Molecular and Cellular Pathology, University of Dundee, Ninewells Hospital and Medical School, Dundee DD1 9SY, UK.
Nucleic Acids Res ; 31(5): 1470-80, 2003 Mar 01.
Article en En | MEDLINE | ID: mdl-12595555
ABSTRACT
The RNA helicases p68 and p72 are highly related members of the DEAD box family of proteins, sharing 90% identity across the conserved core, and have been shown to be involved in both transcription and mRNA processing. We previously showed that these proteins co-localise in the nucleus of interphase cells. In this study we show that p68 and p72 can interact with each other and self-associate in the yeast two-hybrid system. Co-immunoprecipitation experiments confirmed that p68 and p72 can interact in the cell and indicated that these proteins preferentially exist as hetero-dimers. In addition, we show that p68 can interact with NFAR-2, a protein that is also thought to function in mRNA processing. Moreover, gel filtration analysis suggests that p68 and p72 can exist in a variety of complexes in the cell (ranging from approximately 150 to approximately 400 kDa in size), with a subset of p68 molecules being in very large complexes (>2 MDa). The potential to exist in different complexes that may contain p68 and/or p72, together with a range of other factors, would provide the potential for these proteins to interact with different RNA substrates and would be consistent with recent reports implying a wide range of functions for p68/p72.
Asunto(s)

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Fosfoproteínas / Proteínas Quinasas / Adenosina Trifosfatasas / ARN Helicasas Límite: Humans Idioma: En Revista: Nucleic Acids Res Año: 2003 Tipo del documento: Article País de afiliación: Reino Unido

Texto completo: 1 Banco de datos: MEDLINE Asunto principal: Fosfoproteínas / Proteínas Quinasas / Adenosina Trifosfatasas / ARN Helicasas Límite: Humans Idioma: En Revista: Nucleic Acids Res Año: 2003 Tipo del documento: Article País de afiliación: Reino Unido