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U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3′ end processing

Azzouz, Teldja N. ; Gruber, Andreas ; Schümperli, Daniel

In: Nucleic Acids Research, 2005, vol. 33, no. 7, p. 2106-2117

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    Titre
    • U7 snRNP-specific Lsm11 protein: dual binding contacts with the 100 kDa zinc finger processing factor (ZFP100) and a ZFP100-independent function in histone RNA 3′ end processing
    Auteur
    • Azzouz, Teldja N.. Institute of Cell Biology, University of Bern Baltzerstrasse 4, 3012 Bern, Switzerland
    • Gruber, Andreas. Institute of Cell Biology, University of Bern Baltzerstrasse 4, 3012 Bern, Switzerland
    • Schümperli, Daniel. Institute of Cell Biology, University of Bern Baltzerstrasse 4, 3012 Bern, Switzerland
    Type de document
    • Postprint
    Langue
    • Inglese
    Publié dans
    • Nucleic Acids Research, 2005, vol. 33, no. 7, p. 2106-2117. Oxford University Press
    Autre version électronique
    Classification
    • Santé
    Identifiant OAI-PMH
    • oai:doc.rero.ch:300977
    Summary
    The 3′ cleavage generating non-polyadenylated animal histone mRNAs depends on the base pairing between U7 snRNA and a conserved histone pre-mRNA downstream element. This interaction is enhanced by a 100 kDa zinc finger protein (ZFP100) that forms a bridge between an RNA hairpin element upstream of the processing site and the U7 small nuclear ribonucleoprotein (snRNP). The N-terminus of Lsm11, a U7-specific Sm-like protein, was shown to be crucial for histone RNA processing and to bind ZFP100. By further analysing these two functions of Lsm11, we find that Lsm11 and ZFP100 can undergo two interactions, i.e. between the Lsm11 N-terminus and the zinc finger repeats of ZFP100, and between the N-terminus of ZFP100 and the Sm domain of Lsm11, respectively. Both interactions are not specific for the two proteins in vitro, but the second interaction is sufficient for a specific recognition of the U7 snRNP by ZFP100 in cell extracts. Furthermore, clustered point mutations in three phylogenetically conserved regions of the Lsm11 N-terminus impair or abolish histone RNA processing. As these mutations have no effect on the two interactions with ZFP100, these protein regions must play other roles in histone RNA processing, e.g. by contacting the pre-mRNA or additional processing factors