RNA chaperone activity of protein components of human Ro RNPs

RNA - Tập 11 Số 7 - Trang 1084-1094 - 2005
Aurélia Belisova1, Katharina Semrad2, Oliver Mayer2, Grazia Kocian1, Elisabeth Waigmann1, Renée Schroeder2, G Steiner3
1Department of Medical Biochemistry and
2Department of Biochemistry, Max F. Perutz Laboratories, University Departments at the Vienna Biocenter, A-1030 Vienna, Austria
3Department of Medical Biochem-istry, Medical University of Vienna, Vienna Biocenter, Dr. Bohrgasse 9, A-1030 Vienna, Austria;

Tóm tắt

Ro ribonucleoprotein (RNP) complexes are composed of one molecule of a small noncoding cytoplasmic RNA, termed Y RNA, and the two proteins Ro60 and La. Additional proteins such as hnRNP I, hnRNP K, or nucleolin have recently been shown to be associated with subpopulations of Y RNAs. Ro RNPs appear to be localized in the cytoplasm of all higher eukaryotic cells but their functions have remained elusive. To shed light on possible functions of Ro RNPs, we tested protein components of these complexes for RNA chaperone properties employing two in vitro chaperone assays and additionally an in vivo chaperone assay. In these assays the splicing activity of a group I intron is measured. La showed pronounced RNA chaperone activity in thecis-splicing assay in vitro and also in vivo, whereas no activity was seen in thetrans-splicing assay in vitro. Both hnRNP I and hnRNP K exhibited strong chaperone activity in the two in vitro assays, however, proved to be cytotoxic in the in vivo assay. No chaperone activity was observed for Ro60 in vitro and a moderate activity was detected in vivo. In vitro chaperone activities of La and hnRNP I were completely inhibited upon binding of Y RNA. Taken together, these data suggest that the Ro RNP components La, hnRNP K, and hnRNP I possess RNA chaperone activity, while Ro60-Y RNA complexes might function as transporters, bringing other Y RNA binding proteins to their specific targets.

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Tài liệu tham khảo

1995, J. Virol., 69, 6367, 10.1128/jvi.69.10.6367-6375.1995

10.1074/jbc.M001487200

10.1099/vir.0.80045-0

10.1093/emboj/cdg625

10.1101/gad.14.7.777

10.1016/j.cub.2003.11.028

10.1093/emboj/18.13.3776

10.1101/gad.8.13.1575

10.1038/sj.onc.1206645

10.1074/jbc.M201083200

10.1074/jbc.M101360200

1998, Mol. Cell. Biol., 18, 3201, 10.1128/MCB.18.6.3201

10.1016/0378-1119(94)00823-B

10.1016/S0022-2836(02)00518-1

10.1038/sj.emboj.7600058

10.1093/nar/20.14.3671

10.1093/emboj/16.4.793

10.1073/pnas.90.16.7642

10.1074/jbc.270.36.20871

10.1016/S1097-2765(00)00034-4

10.1016/S0168-1702(01)00240-4

1999, Eur. J. Biochem., 266, 151, 10.1046/j.1432-1327.1999.00839.x

10.1128/MCB.20.15.5415-5424.2000

1999, Genetics, 151, 143, 10.1093/genetics/151.1.143

10.1073/pnas.230284297

1995, RNA, 1, 234

2001, J. Gen. Virol., 82, 973, 10.1099/0022-1317-82-5-973

10.1042/BST0301175

1996, Mol. Cell. Biol., 16, 2350, 10.1128/MCB.16.5.2350

10.1016/S1097-2765(03)00093-5

10.1101/gad.8.23.2891

10.1073/pnas.90.15.7250

10.1016/S0092-8674(00)80241-X

10.1128/MCB.22.13.4535-4543.2002

10.1093/emboj/17.24.7442

1993, J. Cell Sci., 106, 929, 10.1242/jcs.106.3.929

10.1006/jmbi.1998.1961

10.1074/jbc.M111798200

10.1128/MCB.24.12.5595-5605.2004

10.1093/nar/19.19.5173

1993, Biochim. Biophys. Acta, 1216, 395, 10.1016/0167-4781(93)90006-Y

1997, Eur. J. Cell. Biol., 74, 123

10.1093/nar/gkg246

10.1017/S1355838201002503

10.1016/0022-2836(90)90264-M

10.1261/rna.7121704

1996, RNA, 2, 769

1996, RNA, 2, 264

10.1038/sj.onc.1207551

1994, J. Virol., 68, 1544, 10.1128/jvi.68.3.1544-1550.1994

1993, J. Biol. Chem., 268, 18249, 10.1016/S0021-9258(17)46837-2

10.1128/MCB.21.10.3281-3288.2001

10.1101/gad.231302

1994, Mol. Cell. Biol., 14, 4509

10.1146/annurev.biochem.71.090501.150003

10.1073/pnas.81.7.1996

10.1093/emboj/19.7.1650

10.1073/pnas.0832411100

10.1016/S0092-8674(00)80220-2

1994, Clin. Rev. Allergy, 12, 253, 10.1007/BF02802321

1995, RNA, 1, 783