Heterodimerization regulates RNase MRP/RNase P association, localization, and expression of Rpp20 and Rpp25

Rpp20 and Rpp25 are subunits of the human RNase MRP and RNase P endoribonucleases belonging to the Alba superfamily of nucleic acid binding proteins. These proteins, which bind very strongly to each other, transiently associate with RNase MRP. Here, we show that the Rpp20-Rpp25 heterodimer is resist...

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Bibliographic Details
Published in:RNA (Cambridge) 2007-01, Vol.13 (1), p.65-75
Main Authors: Welting, Tim J M, Peters, Florence M A, Hensen, Sanne M M, van Doorn, Nienke L, Kikkert, Bastiaan J, Raats, Jos M H, van Venrooij, Walther J, Pruijn, Ger J M
Format: Article
Language:English
Subjects:
Autoantigens - analysis
Autoantigens - genetics
Autoantigens - metabolism
Cell Nucleolus - enzymology
Cells, Cultured
Dimerization
Endoribonucleases - chemistry
Endoribonucleases - genetics
Endoribonucleases - metabolism
Humans
Immunoprecipitation
Ribonuclease P - analysis
Ribonuclease P - chemistry
Ribonuclease P - genetics
Ribonuclease P - metabolism
RNA - metabolism
RNA-Binding Proteins - analysis
RNA-Binding Proteins - genetics
RNA-Binding Proteins - metabolism
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Summary:Rpp20 and Rpp25 are subunits of the human RNase MRP and RNase P endoribonucleases belonging to the Alba superfamily of nucleic acid binding proteins. These proteins, which bind very strongly to each other, transiently associate with RNase MRP. Here, we show that the Rpp20-Rpp25 heterodimer is resistant to both high concentrations of salt and a nonionic detergent. The interaction of Rpp20 and Rpp25 with the P3 domain of the RNase MRP RNA appeared to be strongly enhanced by their heterodimerization. Coimmunoprecipitation experiments demonstrated that only a single copy of each of these proteins is associated with the RNase MRP and RNase P particles in HEp-2 cells. Both proteins accumulate in the nucleoli, which in case of Rpp20 is strongly dependent on its interaction with Rpp25. Finally, the results of overexpression and knock-down experiments indicate that their expression levels are codependent. Taken together, these data indicate that the Rpp20-Rpp25 heterodimerization regulates their RNA-binding activity, subcellular localization, and expression, which suggests that their interaction is also crucial for their role in RNase MRP/P function.
ISSN:1355-8382
1469-9001
DOI:10.1261/rna.237807