The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells

TY - JOUR

T1 - The highly related DEAD box RNA helicases p68 and p72 exist as heterodimers in cells

AU - Ogilvie, V. C.

AU - Wilson, B. J.

AU - Nicol, S. M.

AU - Morrice, N. A.

AU - Saunders, L. R.

AU - Barber, G. N.

AU - Fuller-Pace, F. V.

N1 - dc.publisher: Oxford University Press dc.description.sponsorship: Medical Research Council Biotechnology and Biological Sciences Research Council

PY - 2003/3

Y1 - 2003/3

N2 - 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 ~150 to ~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.

AB - 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 ~150 to ~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.

KW - Adenosine triphosphatases metabolism

KW - Phosphoproteins

KW - Protein kinases metabolism

KW - RNA helicases metabolism

KW - DEAD box protein

KW - p68

KW - p72

U2 - 10.1093/nar/gkg236

DO - 10.1093/nar/gkg236

M3 - Article

SN - 1362-4962

VL - 31

SP - 1470

EP - 1480

JO - Nucleic Acids Research

JF - Nucleic Acids Research

IS - 5

ER -