An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
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ABSTRACT:
SUBMITTER: Doria M
PROVIDER: S-EPMC329436 | biostudies-other | 1991 May
REPOSITORIES: biostudies-other
Publications
An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
Doria M M Carrara G G Calandra P P Tocchini-Valentini G P GP
Nucleic acids research 19910501 9
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. ...[more]
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