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. 2001 Nov;12(11):3680–3689. doi: 10.1091/mbc.12.11.3680

Figure 6.

Figure 6

Association of VSV-hPop4 (mutants) with RNase MRP and RNase P ribonucleoprotein particles and RNase P activity associated with VSV-hPop4 deletion mutants. (A) Constructs encoding (deletion mutants) of VSV-hPop4 were transiently transfected into HEp-2 cells. Extracts from these cells were used for immunoprecipitation with anti-ECFP antibodies. RNA isolated from total cell extracts (lanes 1–8) and immunoprecipitates (lanes 9–16) was analyzed by Northern blot hybridizations with the use of riboprobes specific for RNase MRP and RNase P RNA. Lanes 1 and 9: material from cells transfected with empty vector alone; lanes 2 and 10: VSV-hPop4; lanes 3 and 11: VSV-hPop4 Δ(1–10); lanes 4 and 12: VSV-hPop4 Δ(1–47); lanes 5 and 13: VSV-hPop4 Δ(61–109); lanes 6 and 14: VSV-hPop4 Δ(210–220); lanes 7 and 15: VSV-hPop4 Δ(181–220); and lanes 8 and 16, VSV-hPpop4 Δ(162–220). The positions of RNase MRP and RNase P RNA are indicated on the right. (B) RNase P activity assay associated with immunoprecipitates from extracts of cells transiently transfected with VSV-hPop4 (deletion mutants). Lane 1: material from cells transfected with empty vector alone; lane 2: material from cells expressing VSV-hPop4; lane 3: VSV-hPop4 Δ(1–10); lane 4: VSV-hPpop4 Δ(1–47); lane 5: VSV-hPop4 Δ(61–109); lane 6: VSV-hPop4 Δ(162–220); lane 7: VSV-hPop4 Δ(181–220); lane 8: VSV-hPop4 Δ(210–220); and lane 9: input. On the right, the positions of the pre-tRNA, the mature tRNA and the 5′-leader are indicated.