The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism.

Müller, B; Schümperli, Daniel (1997). The U7 snRNP and the hairpin binding protein: Key players in histone mRNA metabolism. Seminars in cell & developmental biology, 8(6), pp. 567-576. Elsevier 10.1006/scdb.1997.0182

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Animal replication-dependent histone mRNAs are subject to several post-transcriptional regulatory processes. Their non-polyadenylated 3' ends are formed preferentially during S phase by a unique nuclear cleavage event. This requires the base pairing between U7 snRNA and a histone spacer element 3' of the cleavage site. Cleavage occurs preferentially after adenosine, at a fixed distance from the hybrid region. A conserved RNA hairpin just upstream of the cleavage site is recognised by the hairpin binding protein (HBP) that acts as an auxiliary processing factor, stabilising the interaction of the histone pre-mRNA with the U7 snRNP. The interaction between HBP and the RNA hairpin is very stable and HBP is also found associated with histone mRNAs on polysomes. The hairpin and presumably, HBP are also required for nuclear export and translation of histone mRNA. Furthermore, histone mRNAs are selectively destabilised in the G2 phase or upon inhibition of DNA synthesis and this regulation is also associated with the hairpin. Recently, HBP-encoding cDNAs were isolated from various organisms. Human, mouse and Xenopus laevis HBPs are similar, while the Caenorhabditis elegans protein has significant homology to the others only in a central RNA binding domain.Copyright 1997 Academic Press Limited

Item Type:	Journal Article (Original Article)
Division/Institute:	08 Faculty of Science > Department of Biology > Institute of Cell Biology 08 Faculty of Science > Department of Biology > Institute of Cell Biology > RNA
UniBE Contributor:	Schümperli, Daniel
Subjects:	500 Science > 570 Life sciences; biology 500 Science
ISSN:	1096-3634
Publisher:	Elsevier
Language:	English
Submitter:	Daniel Schümperli
Date Deposited:	11 Sep 2015 11:44
Last Modified:	05 Dec 2022 14:49
Publisher DOI:	10.1006/scdb.1997.0182
PubMed ID:	9642171
URI:	https://boris.unibe.ch/id/eprint/71624