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Nucleic Acids Research, 1980, Vol. 8, No. 23 5725-5737
© 1980

MOLECULAR BIOLOGY

Yeast histone mRNA is polyadenylated

K. Fahrner, J. Yarger and L. Hereford*

Department of Biology and Rosenstiel Basic Medical Sciences Research Center, Brandeis University Waltham, MA 02254, USA

*To whom reprint requests should be addressed

Received July 28, 1980. Histone mRNA from S. cerevisiae has been identified and partially purified. The RNA is quantitatively retained on oligo (dT) cellulose or poly(U) sepharose as assayed by in vitro translation or hybridization of radiolabelled cloned yeast histone sequences to RNA immobilized on DBM paper. Retention of yeast histone mRNA on either of these chromatographic systems is most likely the result of polyadenylation since, when primed with oligo (dT), the RNA is an extremely good template for reverse transcriptase, as determined by hybrid arrest translation or by hybridization to D. melanogaster histone DNA sequences.


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