title: Specific binding of a Pop6/Pop7 heterodimer to the P3 stem of the yeast RNase MRP and RNase P RNAs.
abstract: Pop6 and Pop7 are protein subunits of Saccharomyces cerevisiae RNase MRP and RNase P. Here we show that bacterially expressed Pop6 and Pop7 form a soluble heterodimer that binds the RNA components of both RNase MRP and RNase P. Footprint analysis of the interaction between the Pop6/7 heterodimer and the RNase MRP RNA, combined with gel mobility assays, demonstrates that the Pop6/7 complex binds to a conserved region of the P3 domain. Binding of these proteins to the MRP RNA leads to local rearrangement in the structure of the P3 loop and suggests that direct interaction of the Pop6/7 complex with the P3 domain of the RNA components of RNases MRP and P may mediate binding of other protein components. These results suggest a role for a key element in the RNase MRP and RNase P RNAs in protein binding, and demonstrate the feasibility of directly studying RNA-protein interactions in the eukaryotic RNases MRP and P complexes.
authors: Department of Biochemistry and Molecular Biology, The Pennsylvania State University, University Park, Pennsylvania 16802, USA.
authors: Anna
authors: A
authors: Perederina
authors: Olga
authors: O
authors: Esakova
authors: Hasan
authors: H
authors: Koc
authors: Mark E
authors: ME
authors: Schmitt
authors: Andrey S
authors: AS
authors: Krasilnikov
mesh_terms: D001483:Base Sequence; D019281:Dimerization; D004722:Endoribonucleases / Q000737:chemistry / Q000378:metabolism*; D008969:Molecular Sequence Data; D009690:Nucleic Acid Conformation; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D012331:RNA, Fungal / Q000378:metabolism*; D043262:Ribonuclease P / Q000737:chemistry / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000737:chemistry / Q000201:enzymology* / Q000378:metabolism; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry / Q000378:metabolism*
chemical_list: D021122:Protein Subunits; D012331:RNA, Fungal; D029701:Saccharomyces cerevisiae Proteins; D004722:Endoribonucleases; C058330:mitochondrial RNA-processing endoribonuclease; D043262:Ribonuclease P
references: Nucleic Acids Res. 1987 Nov 11;15(21):8783-98
references: 3684574
references: Cell. 1990 Aug 10;62(3):407-9
references: 1696176
references: Genes Dev. 1991 Jul;5(7):1264-76
references: 2065976
references: Mol Cell Biol. 1993 Dec;13(12):7935-41
references: 8247008
references: Genes Dev. 1994 Nov 1;8(21):2617-28
references: 7958920
references: Science. 1996 Apr 12;272(5259):268-70
references: 8602511
references: Genes Dev. 1998 Jun 1;12(11):1678-90
references: 9620854
references: Proc Natl Acad Sci U S A. 1998 Jun 9;95(12):6716-21
references: 9618478
references: Annu Rev Biochem. 1998;67:153-80
references: 9759486
references: RNA. 1999 Apr;5(4):512-24
references: 10199568
references: J Biol Chem. 2005 Mar 25;280(12):11352-60
references: 15637077
references: Nucleic Acids Res. 2005;33(14):4485-95
references: 16087735
references: Crit Rev Biochem Mol Biol. 2006 Mar-Apr;41(2):77-102
references: 16595295
references: Mol Cell. 2006 Nov 3;24(3):445-56
references: 17081993
references: Nucleic Acids Res. 2006;34(18):5145-56
references: 16998185
references: RNA. 2007 Jan;13(1):65-75
references: 17119099
references: Proc Natl Acad Sci U S A. 2007 Feb 13;104(7):2062-7
references: 17284611
references: Gene. 2000 Mar 7;245(1):175-84
references: 10713458
references: RNA. 2000 May;6(5):653-8
references: 10836786
references: RNA. 2000 Dec;6(12):1895-904
references: 11142387
references: RNA. 2001 Apr;7(4):565-75
references: 11345435
references: Proc Natl Acad Sci U S A. 2002 Mar 5;99(5):2684-9
references: 11880623
references: RNA. 2002 Jun;8(6):740-51
references: 12088147
references: Genome Biol. 2003;4(10):R64
references: 14519199
references: Mol Cell Biol. 2004 Feb;24(3):945-53
references: 14729943
references: J Mol Biol. 2004 Aug 6;341(2):375-88
references: 15276830
references: EMBO J. 1987 Feb;6(2):409-17
references: 3582365