| First Author | Moss SB | Year | 1994 |
| Journal | Nucleic Acids Res | Volume | 22 |
| Issue | 15 | Pages | 3160-6 |
| PubMed ID | 8065931 | Mgi Jnum | J:19916 |
| Mgi Id | MGI:68036 | Doi | 10.1093/nar/22.15.3160 |
| Citation | Moss SB, et al. (1994) An alternative pathway of histone mRNA 3' end formation in mouse round spermatids. Nucleic Acids Res 22(15):3160-6 |
| abstractText | 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 non-polyadenylated 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. |
