» Articles » PMID: 2734288

Conserved Terminal Hairpin Sequences of Histone MRNA Precursors Are Not Involved in Duplex Formation with the U7 RNA but Act As a Target Site for a Distinct Processing Factor

Overview
Specialty Science
Date 1989 Jun 1
PMID 2734288
Citations 46
Authors
Affiliations
Soon will be listed here.
Abstract

The hairpin loop structure and the downstream spacer element of histone mRNA precursors are both needed for efficient 3' end formation in vivo and in vitro. Though generally considered as a single processing signal, these two motifs are involved in different types of interaction with the processing machinery. Whereas RNA duplex formation between the downstream spacer element and the U7 small nuclear RNA is essential for processing, we show here that base pairing between the histone stem-loop structure and the U7 RNA is not relevant. Our experiments demonstrate that a processing factor other than the U7 RNA makes contact with the highly conserved hairpin structure of the histone precursor. The recognition of the target site by the processing factor is structure and sequence specific. Prevention of this interaction results in an 80% decrease of 3' cleavage efficiency in vitro. The hairpin binding factor is Sm-precipitable and can be partially separated from the U7 small nuclear ribonucleoprotein particle on a Mono Q column.

Citing Articles

Guard the guardian: A CRL4 ligase stands watch over histone production.

Lampert F, Brodersen M, Peter M Nucleus. 2017; 8(2):134-143.

PMID: 28072566 PMC: 5403139. DOI: 10.1080/19491034.2016.1276143.


Formation of the 3' end of histone mRNA: getting closer to the end.

Dominski Z, Marzluff W Gene. 2007; 396(2):373-90.

PMID: 17531405 PMC: 2888136. DOI: 10.1016/j.gene.2007.04.021.


Human replication-dependent histone H3 genes are activated by a tandemly arranged pair of two CCAAT boxes.

Koessler H, Kahle J, Bode C, Doenecke D, Albig W Biochem J. 2004; 384(Pt 2):317-26.

PMID: 15320874 PMC: 1134115. DOI: 10.1042/BJ20040502.


Evolutionary conservation of the U7 small nuclear ribonucleoprotein in Drosophila melanogaster.

Azzouz T, Schumperli D RNA. 2003; 9(12):1532-41.

PMID: 14624008 PMC: 1370506. DOI: 10.1261/rna.5143303.


The histone 3'-terminal stem-loop-binding protein enhances translation through a functional and physical interaction with eukaryotic initiation factor 4G (eIF4G) and eIF3.

Ling J, Morley S, Pain V, Marzluff W, Gallie D Mol Cell Biol. 2002; 22(22):7853-67.

PMID: 12391154 PMC: 134745. DOI: 10.1128/MCB.22.22.7853-7867.2002.


References
1.
Busslinger M, Portmann R, Birnsteil M . A regulatory sequence near the 3' end of sea urchin histone genes. Nucleic Acids Res. 1979; 6(9):2997-3008. PMC: 327913. DOI: 10.1093/nar/6.9.2997. View

2.
Aziz N, MUNRO H . Iron regulates ferritin mRNA translation through a segment of its 5' untranslated region. Proc Natl Acad Sci U S A. 1987; 84(23):8478-82. PMC: 299567. DOI: 10.1073/pnas.84.23.8478. View

3.
Christie G, Farnham P, Platt T . Synthetic sites for transcription termination and a functional comparison with tryptophan operon termination sites in vitro. Proc Natl Acad Sci U S A. 1981; 78(7):4180-4. PMC: 319752. DOI: 10.1073/pnas.78.7.4180. View

4.
De Robertis E, Lienhard S, Parisot R . Intracellular transport of microinjected 5S and small nuclear RNAs. Nature. 1982; 295(5850):572-7. DOI: 10.1038/295572a0. View

5.
Birchmeier C, Grosschedl R, Birnstiel M . Generation of authentic 3' termini of an H2A mRNA in vivo is dependent on a short inverted DNA repeat and on spacer sequences. Cell. 1982; 28(4):739-45. DOI: 10.1016/0092-8674(82)90053-8. View