Open AccessAn RNA molecule copurifies with RNase P activity fromXenopus laevisoocytes
Author(s) -
Margherita Doria,
G. Carrara,
Patrizia Calandra,
Glauco P. TocchiniValentini
Publication year - 1991
Publication title -
nucleic acids research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 9.008
H-Index - 537
eISSN - 1362-4954
pISSN - 0305-1048
DOI - 10.1093/nar/19.9.2315
Subject(s) - xenopus , biology , rnase p , rna , microbiology and biotechnology , computational biology , genetics , gene
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.