Biochemical demonstration of complex formation of histone pre-mRNA with U7 small nuclear ribonucleoprotein and hairpin binding factors.

Melin, L; Soldati, Dominique; Mital, Renu; Streit, Adrian; Schümperli, Daniel

doi:10.1002/j.1460-2075.1992.tb05101.x

Cited by 59 publications

(59 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Bars represent the average of two or three measurements. Half-lives longer than 3 h (for ribonucleotide reductase, thymidine kinase, proliferating-cell nuclear antigen, and cyclin B1) are extrapolations, because in vitro decay rates are not linear after several hours (55a (34,40,44,72,73,75). The stem-loop region is particularly relevant to histone mRNA degradation for two reasons.…”

Section: Discussionmentioning

confidence: 99%

“…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). In our cell-free mRNA decay system, three factors are required to destabilize polysome-associated histone mRNA: polysomes, histones, and S130.…”

mentioning

confidence: 99%

See 1 more Smart Citation

Human La Protein: a Stabilizer of Histone mRNA

McLaren

Caruccio

Ross

1997

Molecular and Cellular Biology

View full text Add to dashboard Cite

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.

show abstract

Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 99%

Human La Protein: a Stabilizer of Histone mRNA

McLaren

Caruccio

Ross

1997

Molecular and Cellular Biology

View full text Add to dashboard Cite

show abstract

“…Processing of histone pre-mRNAs whose HDE has a relatively weak complementarity to U7 snRNA strongly depends on SLBP. On the other hand, substrates that form strong duplexes with the U7 snRNA can be processed in vitro with a significant efficiency in the absence of SLBP Melin et al, 1992;Spycher et al, 1994;Streit et al, 1993). Under in vivo conditions, SLBP is likely to be an essential factor in processing of all histone pre-mRNAs regardless of the HDE sequence and the extent of base pairing to the U7 snRNA (Pandey et al, 1994).…”

Section: Stem-loop Binding Protein (Slbp)mentioning

confidence: 99%

“…A number of in vitro studies have demonstrated that the role of SLBP in processing is to stabilize binding of U7 snRNP to the HDE Melin et al, 1992;Spycher et al, 1994;Streit et al, 1993). The importance of SLBP in 3' end processing depends on the type of histone pre-mRNA used in the assay.…”

Section: Stem-loop Binding Protein (Slbp)mentioning

confidence: 99%

Formation of the 3′ end of histone mRNA: Getting closer to the end

Domiński

Marzluff

2007

Gene

159

180

View full text Add to dashboard Cite

Nearly all eukaryotic mRNAs end with a poly (A) tail that is added to their 3' end by the ubiquitous cleavage/polyadenylation machinery. The only known exception to this rule are metazoan replication dependent histone mRNAs, which end with a highly conserved stem-loop structure. This distinct 3' end is generated by specialized 3'end processing machinery that cleaves histone pre-mRNAs 4-5 nucleotides downstream of the stem-loop and consists of the U7 small nuclear RNP (snRNP) and number of protein factors. Recently, the U7 snRNP has been shown to contain a unique Sm core that differs from that of the spliceosomal snRNPs, and an essential heat labile processing factor has been identified as symplekin. In addition, cross-linking studies have pinpointed CPSF-73 as the endonuclease, which catalyzes the cleavage reaction. Thus, many of the critical components of the 3' end processing machinery are now identified. Strikingly, this machinery is not as unique as initially thought but contains a number of factors involved in cleavage/polyadenylation, suggesting that the two mechanisms have a common evolutionary origin. The greatest challenge that lies ahead is to determine how all these factors interact with each other to form a catalytically competent processing complex capable of cleaving histone pre-mRNAs.

show abstract

“…Because the replication-dependent histone genes do not have introns, the only processing reaction required for the formation of mature histone mRNA is cleavage to form the 3' end. Processing of the 3' end of histone mRNA requires two cis elements, the stem-loop that interacts with a factor termed the hairpin binding factor (HBF) (Mowry and Steitz 1987a;Vasserot et al 1989;Melin et al 1992), and a purine-rich sequence located 9-14 nucleotides 3' of the stem-loop that binds the U7 small nuclear ribonucleoprotein particle (snRNP) (Mowry and Steitz 1987b;Cotten et al 1988;Soldati and Schiimperli 1988;Bond et al 1991). In addition to these two trans-acting factors, there is a heat-labile factor that has not been well characterized (Gick et al 1987).…”

mentioning

confidence: 99%

The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing.

Wang¹,

Whitfield²,

Ingledue³

et al. 1996

Genes Dev.

249

262

View full text Add to dashboard Cite

Replication-dependent histone mRNAs are not polyadenylated but end in a conserved 26-nucleotide structure that contains a stem-loop. Much of the cell cycle regulation of histone mRNA is post-transcriptional and is mediated by the 3' end of histone mRNA. The stem-loop binding protein (SLBP) that binds the 3' end of histone mRNA is a candidate for the factor that participates in most, if not all, of the post-transcriptional regulatory events. We have cloned the cDNA for the SLBP from humans, mice, and frogs, using the recently developed yeast three-hybrid system. The human SLBP is a 31-kD protein and contains a novel RNA-binding domain, which has been mapped to a 73-amino-acid region of the protein. The cloned SLBP is the protein bound to the 3' end of histone mRNA as antibodies specific for the SLBP remove all specific binding activity from nuclear and polyribosomal extracts. These depleted extracts do not cleave histone pre-mRNA efficiently, demonstrating that the SLBP is required for efficient histone pre-mRNA processing.

show abstract

Biochemical demonstration of complex formation of histone pre-mRNA with U7 small nuclear ribonucleoprotein and hairpin binding factors.

Cited by 59 publications

References 24 publications

Human La Protein: a Stabilizer of Histone mRNA

Human La Protein: a Stabilizer of Histone mRNA

Formation of the 3′ end of histone mRNA: Getting closer to the end

The protein that binds the 3' end of histone mRNA: a novel RNA-binding protein required for histone pre-mRNA processing.

Contact Info

Product

Resources

About