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. 1991 May 11;19(9):2315–2320. doi: 10.1093/nar/19.9.2315

An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.

M Doria 1, G Carrara 1, P Calandra 1, G P Tocchini-Valentini 1
PMCID: PMC329436  PMID: 1710353

Abstract

Utilizing a procedure for the purification of RNase P from Xenopus laevis germinal vesicle (GV) extracts, according to which the contamination by a large, cytoplasmic, cylindrical structure (1) is avoided, we demonstrate that the X.laevis enzyme, like the HeLa RNase P, is precipitated by anti-Th antibodies and an RNA molecule (XL RNA), 320 nucleotides long, copurifies with the activity. The sequence of XL RNA is 60% homologous to HeLa H1 RNA, therefore the two molecules seem related.

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Selected References

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