Nucleic Acids Research, 1994, Vol. 22, No. 15 3160-3166
© 1994
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An alternative pathway of histone mRNA 3' end formation in mouse round spermatids
1 Division of Reproductive Biology, Department of Obstetrics and Gynecology, and Department of Cell and Developmental Biology, University of Pennsylvania School of Medicine Philadelphia, PA 19104 2 Division of Basic Sciences, Fred Hutchinson Cancer Research Center Seattle, WA 98104 Department of Radiation Oncology, University of Washington School of Medicine Seattle, WA 98195
* To whom correspondence should be addressed
Received March 29, 1994. Revised June 14, 1994. Accepted June 14, 1994.
During mammalian spermiogenesis, the post-meiotic stage of spermatogenesis, histones are replaced by protamines on the DNA. Despite this histone elimination, novel polyadenylated histone transcripts were detected in mouse round spermatids. Sequence analysis of a spermatid-specific H2a cDNA clone indicated that it was derived from a mRNA of a replication-dependent histone gene even though its transcript was not polyadenylated in somatic and earlier spermatogenic cells. In round spermatids, both the hairpin and purine-rich elements in the 3' untranslated region of the somatic pre-mRNA were retained in the mature poly(A)+ mRNA transcripts. Polyadenylation occurred downstream of the purine-rich element and was not preceded by the somatic AATAAA polyadenylation signal sequence. While polyadenylated histone transcripts from replication-dependent genes have been observed previously in somatic cells, characteristics of this type of 3'-end formation in mammalian round spermatids were unique. In particular, a specific replication-dependent H2a gene was transcribed either as a polyadenylated or nonpolyadenylated transcript in these cells, suggesting that the type of transcript present was dependent on the RNA sequence. Finally, both poly(A) and poly(A)+ mRNAs were found on polyribosomes from round spermatids, indicating that histones were being translated in these cells and that the polyadenylation status of these transcripts did not affect their translatability.
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