Coupling of replication type histone mRNA levels to DNA synthesis requires the stem-loop sequence at the 3' end of the mRNA.

Levine, B J; Chodchoy, Nunta; Marzluff, William F.; Skoultchi, Arthur I.

doi:10.1073/pnas.84.17.6189

Cited by 118 publications

(87 citation statements)

References 29 publications

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“…In contrast, in somatic cells both types of mRNAs are transcribed from a single gene with the polyadenylated transcript being an extremely small proportion of the total RNA produced from that gene (e.g. see 26). Furthermore, these findings in the mouse differed from the avian system where only poly(A)+ histone mRNAs are present in round spermatids (29).…”

Section: Discussioncontrasting

confidence: 41%

“…Furthermore, while an increase in poly(A) length has been described for some RNAs in early embryogenesis as a method for translational activation (for review see 25), the histone transcripts described in this report do not contain cytoplasmic polyadenylation elements. While polyadenylated histone transcripts from replicationdependent genes have been described previously (including those from the H2a.614 gene) in both vertebrate somatic (23,(26)(27)(28) and spermatogenic cells (29), characteristics of the 3'-end formation observed in mouse spermatogenic cells were unique. First, although both polyadenylated and non-polyadenylated histone transcripts were present in round spermatids, a particular H2a gene was transcribed as either one or the other type of transcript.…”

Section: Discussionmentioning

confidence: 99%

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

1994

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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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Section: Discussioncontrasting

confidence: 41%

Section: Discussionmentioning

confidence: 99%

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

1994

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“…In some cases, such mRNAs represent a very minor part of the total mRNA pool (Levine et al, 1987). In several histone H I transcripts in chicken (Kirsh et al, 1989) and mouse (Cheng et al, 1989), as well as in transcripts encoding the histone H2A.X variant (Mannironi et al, 1989;Nagata et al, 1991), the two modes of the 3' processing occur with comparable efficiency in the same cell or tissue type.…”

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confidence: 99%

Two Types of Polyadenated mRNAs are Synthesized from Drosophila Replication‐Dependent Histone Genes

Akhmanova¹,

Miedema²,

Kremer³

et al. 1997

European Journal of Biochemistry

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The polyadenylation of replication-dependent histone H2B, H 3 and H4 mRNAs in Drosophilu melanoguster was analysed. Two types of mRNAs, containing a poly(A) tail, can be detected in addition to non-polyadenylated messengers, which represent the majority of replication-dependent histone mRNAs. Firstly, conventional polyadenylation signals, localized downstream from the stem-loop region, are used to produce polyadenylated mRNAs. The messengers of this type, generated from the D. melanogaster H2B gene, are preferentially synthesized in the testis of the fly. Secondly, a distinct type of polyadenylated histone mRNA has been identified. This mRNA, which is present in many different tissues and constitutes a minor part of the total histone mRNA pool, contains a short poly(A) tail, added to the end of the 3' terminal stem-loop structure, which is in most cases lacking several nucleotides from its 3' end. The sites of polyadenylation within the stem-loop are not preceded by a nornial polyadenylation signal. The possible functions of the polyadenylated histone transcripts are discussed.

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“…1B). The stem-loop is essential for proper cell cycle regulation and is the site at which mRNA degradation begins (4,14,29,31,39,47,56,57,65,68,75). It is also a binding site for a unique stemloop binding protein (40,46,72,73,76).…”

mentioning

confidence: 99%

“…Specificity is achieved primarily via the unique 3Ј-terminal structure of histone mRNA. The 3Ј terminus lacks poly(A) and contains a 6-bp stem and 4-base loop (29,31,45) (see Fig. 1B).…”

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confidence: 99%

Human La Protein: a Stabilizer of Histone mRNA

McLaren

Caruccio

Ross

1997

Molecular and Cellular Biology

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Histone mRNA is destabilized at the end of S phase and in cell-free mRNA decay reaction mixtures supplemented with histone proteins, indicating that histones might autoregulate the histone mRNA half-life. Histone mRNA destabilization in vitro requires three components: polysomes, histones, and postpolysomal supernatant (S130). Polysomes are the source of the mRNA and mRNA-degrading enzymes. To investigate the role of the S130 in autoregulation, crude S130 was fractionated by histone-agarose affinity chromatography. Two separate activities affecting the histone mRNA half-life were detected. The histone-agarose-bound fraction contained a histone mRNA destabilizer that was activated by histone proteins; the unbound fraction contained a histone mRNA stabilizer. Further chromatographic fractionation of unbound material revealed only a single protein stabilizer, which was purified to homogeneity, partially sequenced, and found to be La, a wellcharacterized RNA-binding protein. When purified La was added to reaction mixtures containing polysomes, a histone mRNA decay intermediate was stabilized. This intermediate corresponded to histone mRNA lacking 12 nucleotides from its 3 end and containing an intact coding region. Anti-La antibody blocked the stabilization effect. La had little or no effect on several other cell cycle-regulated mRNAs. We suggest that La prolongs the histone mRNA half-life during S phase and thereby increases histone protein production.

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Coupling of replication type histone mRNA levels to DNA synthesis requires the stem-loop sequence at the 3' end of the mRNA.

Cited by 118 publications

References 29 publications

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

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

Two Types of Polyadenated mRNAs are Synthesized from Drosophila Replication‐Dependent Histone Genes

Human La Protein: a Stabilizer of Histone mRNA

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