Each of the Conserved Sequence Elements Flanking the Cleavage Site of Mammalian Histone Pre-mRNAs Has a Distinct Role in the 3′-End Processing Reaction

Mowry, Kimberly L.; Oh, Rosemary; Steitz, Joan A.

doi:10.1128/mcb.9.7.3105-3108.1989

Cited by 7 publications

(4 citation statements)

References 30 publications

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“…The nuclear SLBP is detected efficiently by the mobility-shift assay , suggesting that it is not bound to histone mRNA. The stem-loop at the 3′ end of histone mRNA is also important in processing of the 3′ end of histone mRNA, and there is a hairpin-binding factor involved in the 3′ end formation that recognizes the stem-loop (Melin et al, 1992;Vasserot et al, 1989;Mowry et al, 1989;Mowry & Steitz, 1987). Recently, we have shown that the polyribosomal SLBP can complement a nuclear processing extract deficient in the hairpin-binding factor (Dominski et al, 1995), suggesting that the SLBP is the hairpin-binding factor (or part of the hairpin-binding factor) required for histone 3′ end formation.…”

Section: Discussionmentioning

confidence: 99%

“…The polyA sequence present at the 3′ end of most mRNAs has a number of functions in mRNA metabolism, which are mediated by interaction with the polyA binding protein (Sachs et al, 1987;Sachs & Davis, 1989;Bernstein & Ross, 1989;Jackson & Standart, 1990), including participating in translation (Gallie, 1991;McGrew & Richter, 1990;Munroe & Jacobson, 1990) and contributing to mRNA stability. Similarly, the 3′ end of histone mRNA is involved in mRNA processing (Melin et al, 1992;Vasserot et al, 1989;Mowry et al, 1989), transport (Williams et al, 1994), translation (Sun et al, 1992) and regulation of stability (Sun et al, 1992;Marzluff, 1992). These functions are likely mediated by interaction with specific protein(s).…”

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confidence: 99%

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Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

et al. 1996

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Replication-dependent histone mRNAs end in a highly conserved stem-loop sequence rather than a polyA sequence. A 45-kDa stem-loop binding protein (SLBP), which specifically binds the stem-loop of histone mRNA, is present in both polyribosomes and nuclei. An identical 45-kDa protein, as determined by partial protease digestion, is cross-linked to a 30 nt RNA containing the 3' stem-loop from both nuclei and polyribosomes. The SLBP can also be detected by a Northwestern blot procedure using the 30 nt RNA as a probe. As judged from the Northwestern assay, more than 90% of the SLBP in the cell is found in the polyribosomes with the remaining SLBP localized to the nucleus. Only 5-10% of the SLBP could be extracted from the polyribosomes with salt. Treatment of the polyribosomes with micrococcal nuclease prior to salt extraction solubilized 5-10 times more SLBP as an RNA-protein complex. The SLBP could be subsequently partially purified from this complex.

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Section: Discussionmentioning

confidence: 99%

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Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

et al. 1996

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“…Since this finding was not compatible with previous reports of replication-dependent histone mRNAs in higher vertebrates, we isolated the corresponding genomic clone. The genomic sequence contained both the classical hairpin loop structure and the conserved downstream purine-rich element, which interacted with U7 nuclear RNA in the 3'-end processing of the nonpolyadenylated histone pre-mRNAs (38). Immediately upstream from the hairpin loop the genomic clone contained an oligo[d (A4GA10)] sequence on the DNA strand corresponding to the mRNA sequence.…”

Section: Discussionmentioning

confidence: 99%

“…Numerous studies in which altered sequences of several histone genes have been used have been performed to elucidate the molecular mechanisms and the sequence motifs essential for cell-cycle-dependent regulation of the replication-dependent histone mRNAs (1,22,30,33,38). The abundantly expressed histone H2A.1 gene characterized in this paper might also be valuable for further studies on the regulation of mRNA expression.…”

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A Genomic Clone Encoding a Novel Proliferation-Dependent Histone H2A.1 mRNA Enriched in the Poly(A)⁺ Fraction

Fecker

Ekblom

Kurkinen

et al. 1990

Molecular and Cellular Biology

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Replication-dependent histone mRNAs are prime examples of nonpolyadenylated mRNAs. We isolated and characterized cDNAs and a genomic clone for a replication-dependent histone H2A.1 mRNA which segregated into the poly(A)+ fraction during mRNA isolation through an oligo(dT)-cellulose column. However, the results of sequencing of the genomic clone suggested that the mRNA did not contain a poly(A) tail. Instead, the genomic sequence revealed a nonterminal oligo(A) tract directly upstream from the typical 3'-terminal hairpin loop of replication-dependent histone mRNAs. The nonterminal oligo(A) tract consisted of 14 adenylate residues interrupted by one guanylate residue (A4GA10). We concluded that this short oligo(A) stretch mediated binding of the mRNA to oligo(dT) even after stringent washes with 0.1 M NaCl, indicating that rather short oligo(A) sequences can ensure binding to oligo(dT)-cellulose. The cDNA and genomic clones contained an AAATAAG sequence at the end of the coding region. It has been suggested that this sequence contains a polyadenylation signal in some yeast and mouse transcripts, but it does not function as a polyadenylation signal in the histone transcript described in this paper.

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Length suppression in histone messenger RNA 3′-end maturation: Processing defects of insertion mutant premessenger RNAs can be compensated by insertions into the U7 small nuclear RNA

Scharl

Steitz

1996

Proc. Natl. Acad. Sci. U.S.A.

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Efficient 3-end processing of cell cycleregulated mammalian histone premessenger RNAs (premRNAs) requires an upstream stem-loop and a histone downstream element (HDE) that base pairs with the U7 small ribonuclearprotein. Insertions between these elements have two effects: the site of cleavage moves in concert with the HDE and processing efficiency declines. We used Xenopus oocytes to ask whether compensatory length insertions in the human U7 RNA could restore the fidelity and efficiency of processing of mouse histone insertion pre-mRNAs. An insertion of 5 nt into U7 RNA that extends its complementary to the HDE compensated for both defects in processing of a 5-nt insertion substrate; a noncomplementary insertion into U7 did not. Yet, the noncomplementary insertion mutant U7 was shown to be active on insertion substrates further mutated to allow base pairing. Our results suggest that the histone pre-mRNA becomes rigidified upstream of its HDE, allowing the bound U7 small ribonucleoprotein to measure from the HDE to the cleavage site. Such a mechanism may be common to other RNA measuring systems. To our knowledge, this is the first demonstration of length suppression in an RNA processing system.Cell cycle-regulated histone premessenger RNAs (premRNAs) are unusual RNA polymerase II transcripts because they do not contain introns and are not polyadenylylated (for review, see refs. 1 and 2). Instead, their 3Ј ends are formed by endonucleolytic cleavage. Two conserved elements on the histone pre-mRNA are required for efficient processing: a stem-loop structure found directly upstream of the site of cleavage and a purine-rich region located 9-17 nt (usually 11 Ϯ 1 nt, see ref.3) downstream of the cleavage site termed the histone downstream element (HDE) (Fig. 1). There are at least three trans-acting factors involved in histone mRNA maturation: a factor that binds the stem-loop element (7-11), an essential heat-labile factor whose role is not yet understood (12-14), and the low-abundance U7 small nuclear ribonucleoprotein (snRNP) (for reviews, see refs. 15 and 16), which contains at least two proteins of 50 kDa and 14 kDa (17-19) in addition to the core Sm proteins (20). Genetic suppression experiments established that the 5Ј end of the U7 RNA base pairs with the purines of the HDE during histone pre-mRNA processing (6, 21) (see Fig. 1); the ability to form an small nuclear RNA (snRNA)-pre-mRNA duplex, rather than the exact sequence of the complementary regions, is critical for processing.Previously, we reported the effects of systematically moving the HDE further downstream of the stem-loop in a mouse histone H2A pre-mRNA (22). The processed products generated in a HeLa cell in vitro system revealed that the site of 3Ј-end formation moves in concert with the movement of the HDE, remaining 11 Ϯ 1 nt upstream. Decreases in processing efficiency were also observed as the HDE was distanced from the stem-loop. These results suggested that the U7 snRNP directs cleavage at a fixed distance from its binding site (term...

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Each of the Conserved Sequence Elements Flanking the Cleavage Site of Mammalian Histone Pre-mRNAs Has a Distinct Role in the 3′-End Processing Reaction

Cited by 7 publications

References 30 publications

Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

A Genomic Clone Encoding a Novel Proliferation-Dependent Histone H2A.1 mRNA Enriched in the Poly(A)⁺ Fraction

Length suppression in histone messenger RNA 3′-end maturation: Processing defects of insertion mutant premessenger RNAs can be compensated by insertions into the U7 small nuclear RNA

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Each of the Conserved Sequence Elements Flanking the Cleavage Site of Mammalian Histone Pre-mRNAs Has a Distinct Role in the 3′-End Processing Reaction

Cited by 7 publications

References 30 publications

Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

Efficient Extraction and Partial Purification of the Polyribosome-Associated Stem−Loop Binding Protein Bound to the 3‘ End of Histone mRNA

A Genomic Clone Encoding a Novel Proliferation-Dependent Histone H2A.1 mRNA Enriched in the Poly(A)+ Fraction

Length suppression in histone messenger RNA 3′-end maturation: Processing defects of insertion mutant premessenger RNAs can be compensated by insertions into the U7 small nuclear RNA

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A Genomic Clone Encoding a Novel Proliferation-Dependent Histone H2A.1 mRNA Enriched in the Poly(A)⁺ Fraction