On the existence of polyadenylated histone mRNA in Xenopus laevis oocytes.
In a variety of systems, histone mRNA has been shown to lack poly(A) (Adesnik and Darnell, 1972; Grunstein et al., 1973). We have found, however, that in Xenopus laevis oocytes, poly (A)-containing mRNA codes for histones, in a wheat germ cell-free system, based on the following criteria: first, co-migration with authentic X. laevis oocyte histones on polyacrylamide gels; second, no detectable incorporation of tryptophan; third, differential incorporation of lysine and methionine into histone fraction H2A; fourth, resistance of histone fraction H2A to cleavage with cyanogen bromide; and fifth, correspondence of tryptic peptide maps of partially purified cell-free products with authentic X. laevis oocyte histone. RNA which directs the synthesis of histones in the cell-free system is retained on oligo(dT)-cellulose, even after denaturation in 80% DMSO at 70 degrees C, thereby demonstrating the covalent attachment of polyadenylic acid sequences to the mRNA. Poly (A)- RNA (7S-14S fraction) was also found to code for histones using the same criteria. We discuss the significance of the finding that X. laevis oocytes contain two classes of histone mRNA as well as the potential developmental implications of this observation.
D000818:Animals; D002474:Cell-Free System; D002845:Chromatography; D003488:Cyanogen Bromide / Q000494:pharmacology; D004121:Dimethyl Sulfoxide / Q000494:pharmacology; D005260:Female; D006657:Histones / Q000032:analysis / Q000096:biosynthesis*; D008239:Lysine / Q000378:metabolism; D008715:Methionine / Q000378:metabolism; D009865:Oocytes / Q000378:metabolism*; D010063:Ovum / Q000378:metabolism*; D011061:Poly A; D014176:Protein Biosynthesis; D012333:RNA, Messenger / Q000032:analysis / Q000378:metabolism*; D014364:Tryptophan / Q000378:metabolism; D014981:Xenopus
D006657:Histones; D012333:RNA, Messenger; D011061:Poly A; D014364:Tryptophan; D008715:Methionine; D008239:Lysine; D003488:Cyanogen Bromide; D004121:Dimethyl Sulfoxide