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

被引:71
作者
Ogilvie, VC
Wilson, BJ
Nicol, SM
Morrice, NA
Saunders, LR
Barber, GN
Fuller-Pace, FV [1 ]
机构
[1] Univ Dundee, Ninewells Hosp & Med Sch, Dept Mol & Cellular Pathol, Dundee DD1 9SY, Scotland
[2] Univ Dundee, Sch Life Sci, MRC, Prot Phosphorylat Unit, Dundee DD1 5EH, Scotland
[3] Univ Miami, Sch Med, Sylvester Comprehens Canc Ctr, Dept Microbiol & Immunol, Miami, FL 33136 USA
关键词
D O I
10.1093/nar/gkg236
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
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 similar to150 to similar to400 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.
引用
收藏
页码:1470 / 1480
页数:11
相关论文
共 41 条
[11]   DETECTION OF DSRNA-BINDING DOMAINS IN RNA HELICASE-A AND DROSOPHILA MALELESS - IMPLICATIONS FOR MONOMERIC RNA HELICASES [J].
GIBSON, TJ ;
THOMPSON, JD .
NUCLEIC ACIDS RESEARCH, 1994, 22 (13) :2552-2556
[12]   RNA HELICASE ACTIVITY ASSOCIATED WITH THE HUMAN P68 PROTEIN [J].
HIRLING, H ;
SCHEFFNER, M ;
RESTLE, T ;
STAHL, H .
NATURE, 1989, 339 (6225) :562-564
[13]   Regulation of alternative splicing by the ATP-dependent DEAD-box RNA helicase p72 [J].
Hönig, A ;
Auboeuf, D ;
Parker, MM ;
O'Malley, BW ;
Berget, SM .
MOLECULAR AND CELLULAR BIOLOGY, 2002, 22 (16) :5698-5707
[14]   The ATPase, RNA unwinding, and RNA binding activities of recombinant p68 RNA helicase [J].
Huang, YL ;
Liu, ZR .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (15) :12810-12815
[15]   NUCLEAR PROTEIN-P68 IS AN RNA-DEPENDENT ATPASE [J].
IGGO, RD ;
LANE, DP .
EMBO JOURNAL, 1989, 8 (06) :1827-1831
[16]   P68 RNA HELICASE - IDENTIFICATION OF A NUCLEOLAR FORM AND CLONING OF RELATED GENES CONTAINING A CONSERVED INTRON IN YEASTS [J].
IGGO, RD ;
JAMIESON, DJ ;
MACNEILL, SA ;
SOUTHGATE, J ;
MCPHEAT, J ;
LANE, DP .
MOLECULAR AND CELLULAR BIOLOGY, 1991, 11 (03) :1326-1333
[17]   Developmental and tissue-specific expression of DEAD box protein p72 [J].
Ip, FCF ;
Chung, SSK ;
Fu, WY ;
Ip, NY .
NEUROREPORT, 2000, 11 (03) :457-462
[18]   Crystallographic structure of the amino terminal domain of yeast initiation factor 4A, a representative DEAD-box RNA helicase [J].
Johnson, ER ;
McKay, DB .
RNA, 1999, 5 (12) :1526-1534
[19]   A chicken embryo protein related to the mammalian DEAD box protein p68 is tightly associated with the highly purified protein-RNA complex of 5-MeC-DNA glycosylase [J].
Jost, JP ;
Schwarz, S ;
Hess, D ;
Angliker, H ;
Fuller-Pace, FV ;
Stahl, H ;
Thiry, S ;
Siegmann, M .
NUCLEIC ACIDS RESEARCH, 1999, 27 (16) :3245-3252
[20]   Expression of p68 RNA helicase is closely related to the early stage of adipocyte differentiation of mouse 3T3-L1 cells [J].
Kitamura, A ;
Nishizuka, M ;
Tominaga, K ;
Tsuchiya, T ;
Nishihara, T ;
Imagawa, M .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 2001, 287 (02) :435-439