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. 1997 Jun;17(6):3028-36.
doi: 10.1128/MCB.17.6.3028.

Human La protein: a stabilizer of histone mRNA

R S McLaren  1 , N Caruccio, J Ross
Affiliations

Human La protein: a stabilizer of histone mRNA

R S McLaren et al. Mol Cell Biol. 1997 Jun.

Abstract

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 well-characterized 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.

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References

    1. EMBO J. 1989 Mar;8(3):851-61 - PubMed
    1. Proc Natl Acad Sci U S A. 1989 Jun;86(12):4345-9 - PubMed
    1. Nucleic Acids Res. 1989 Oct 25;17(20):8061-71 - PubMed
    1. Biochim Biophys Acta. 1991 Mar 26;1088(3):327-39 - PubMed
    1. Annu Rev Biochem. 1991;60:827-61 - PubMed

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