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- W1582302014 abstract "During spermatogenesis, somatic histones are partially replaced by testis-specific subtypes appearing together with transition proteins. In haploid spermatids, both histones and transition proteins are replaced by protamines. DNA-protamine interactions result in chromatin condensation causing cessation of transcription in elongating spermatids. This occurs at a time when many proteins need to be synthesized and assembled for the complete condensation of the chromatin, the development of the acrosome, and the formation of the flagellum. To ensure complete differentiation of round spermatids into mature spermatozoa, the precise temporal regulation of gene expression via transcriptional and translational control mechanisms is of pivotal importance. These processes involve the binding of transcription factors to the promoter sequence of the genes and protein repressors to the 3′-untranslated region and poly-A tail of the transcripts. Human male infertility has been associated with both decreased levels of protamines and increased protamine-1 to protamine-2 ratios. These findings are in line with data obtained from haploinsufficient mice carrying a mutation in either protamine-1 or protamine-2 resulting in male sterility. Despite some species-specific peculiarities, there is broad conformity between human and murine spermatogenesis recommending mouse an excellent animal model for the study of human spermatogenesis. To further unravel the mechanisms being involved in the regulation of gene expression during spermatogenesis, knockout and transgenic mice will play an important role in answering questions about the function of a specific gene and the sequences being responsible for the manner in which this gene is expressed during spermatogenesis." @default.
- W1582302014 created "2016-06-24" @default.
- W1582302014 creator A5025101056 @default.
- W1582302014 date "2002-01-01" @default.
- W1582302014 modified "2023-10-14" @default.
- W1582302014 title "Gene expression during mouse spermatogenesis" @default.
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