An RNA molecule copurifies with RNase P activity from Xenopus laevis oocytes.
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.
Doria
M
M
Enimont, Dipartimento di Biotecnologie, Rome, Italy.
Carrara
G
G
Calandra
P
P
Tocchini-Valentini
G P
GP
D000818:Animals; D001483:Base Sequence; D002458:Cell Fractionation; D002499:Centrifugation, Density Gradient; D004722:Endoribonucleases / Q000302:isolation & purification* / Q000378:metabolism; D006367:HeLa Cells; D006801:Humans; D008969:Molecular Sequence Data; D011233:Precipitin Tests; D012313:RNA / Q000302:isolation & purification* / Q000378:metabolism; D016337:RNA, Catalytic / Q000302:isolation & purification* / Q000378:metabolism; D043262:Ribonuclease P; D012689:Sequence Homology, Nucleic Acid; D014982:Xenopus laevis
D016337:RNA, Catalytic; D012313:RNA; D004722:Endoribonucleases; C468368:RPP14 protein, human; D043262:Ribonuclease P