Literature DB >> 8065931

An alternative pathway of histone mRNA 3' end formation in mouse round spermatids.

S B Moss1, R A Ferry, M Groudine.   

Abstract

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.

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Year:  1994        PMID: 8065931      PMCID: PMC310291          DOI: 10.1093/nar/22.15.3160

Source DB:  PubMed          Journal:  Nucleic Acids Res        ISSN: 0305-1048            Impact factor:   16.971


  32 in total

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Journal:  Dev Biol       Date:  1976-03       Impact factor: 3.582

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3.  Different 3'-end processing produces two independently regulated mRNAs from a single H1 histone gene.

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Journal:  Proc Natl Acad Sci U S A       Date:  1989-09       Impact factor: 11.205

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Authors:  D T Brown; S E Wellman; D B Sittman
Journal:  Mol Cell Biol       Date:  1985-11       Impact factor: 4.272

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Authors:  J D Taylor; S E Wellman; W F Marzluff
Journal:  J Mol Evol       Date:  1986       Impact factor: 2.395

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Authors:  K C Kleene; R J Distel; N B Hecht
Journal:  Dev Biol       Date:  1984-09       Impact factor: 3.582

7.  The consensus sequence YGTGTTYY located downstream from the AATAAA signal is required for efficient formation of mRNA 3' termini.

Authors:  J McLauchlan; D Gaffney; J L Whitton; J B Clements
Journal:  Nucleic Acids Res       Date:  1985-02-25       Impact factor: 16.971

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Journal:  J Biol Chem       Date:  1983-07-25       Impact factor: 5.157

9.  Faithful cell-cycle regulation of a recombinant mouse histone H4 gene is controlled by sequences in the 3'-terminal part of the gene.

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Journal:  Proc Natl Acad Sci U S A       Date:  1985-07       Impact factor: 11.205

10.  The conserved CAAGAAAGA spacer sequence is an essential element for the formation of 3' termini of the sea urchin H3 histone mRNA by RNA processing.

Authors:  O Georgiev; M L Birnstiel
Journal:  EMBO J       Date:  1985-02       Impact factor: 11.598

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  9 in total

1.  Intronless mRNA transport elements may affect multiple steps of pre-mRNA processing.

Authors:  Y Huang; K M Wimler; G G Carmichael
Journal:  EMBO J       Date:  1999-03-15       Impact factor: 11.598

2.  Two distinct forms of the 64,000 Mr protein of the cleavage stimulation factor are expressed in mouse male germ cells.

Authors:  A M Wallace; B Dass; S E Ravnik; V Tonk; N A Jenkins; D J Gilbert; N G Copeland; C C MacDonald
Journal:  Proc Natl Acad Sci U S A       Date:  1999-06-08       Impact factor: 11.205

3.  Early evolution of histone mRNA 3' end processing.

Authors:  Marcela Dávila López; Tore Samuelsson
Journal:  RNA       Date:  2007-11-12       Impact factor: 4.942

4.  Developmental control of histone mRNA and dSLBP synthesis during Drosophila embryogenesis and the role of dSLBP in histone mRNA 3' end processing in vivo.

Authors:  David J Lanzotti; Handan Kaygun; Xiao Yang; Robert J Duronio; William F Marzluff
Journal:  Mol Cell Biol       Date:  2002-04       Impact factor: 4.272

5.  Organization and expression of bovine TSPY.

Authors:  T Vogel; F Dechend; E Manz; C Jung; S Jakubiczka; S Fehr; J Schmidtke; F Schnieders
Journal:  Mamm Genome       Date:  1997-07       Impact factor: 2.957

6.  Stem-loop binding protein expressed in growing oocytes is required for accumulation of mRNAs encoding histones H3 and H4 and for early embryonic development in the mouse.

Authors:  Daniel R Arnold; Patricia Françon; James Zhang; Kyle Martin; Hugh J Clarke
Journal:  Dev Biol       Date:  2007-10-28       Impact factor: 3.582

7.  Knockdown of SLBP results in nuclear retention of histone mRNA.

Authors:  Kelly D Sullivan; Thomas E Mullen; William F Marzluff; Eric J Wagner
Journal:  RNA       Date:  2009-01-20       Impact factor: 4.942

8.  CstF-64 supports pluripotency and regulates cell cycle progression in embryonic stem cells through histone 3' end processing.

Authors:  Bradford A Youngblood; Petar N Grozdanov; Clinton C MacDonald
Journal:  Nucleic Acids Res       Date:  2014-06-23       Impact factor: 16.971

9.  A subset of replication-dependent histone mRNAs are expressed as polyadenylated RNAs in terminally differentiated tissues.

Authors:  Shawn M Lyons; Clark H Cunningham; Joshua D Welch; Beezly Groh; Andrew Y Guo; Bruce Wei; Michael L Whitfield; Yue Xiong; William F Marzluff
Journal:  Nucleic Acids Res       Date:  2016-07-08       Impact factor: 16.971

  9 in total

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