hnRNP F Influences Binding of a 64-Kilodalton Subunit of Cleavage Stimulation Factor to mRNA Precursors in Mouse B Cells

doi:10.1128/MCB.21.4.1228-1238.2001

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Molecular and Cellular Biology, February 2001, p. 1228-1238, Vol. 21, No. 4
0270-7306/01/$04.00+0 DOI: 10.1128/MCB.21.4.1228-1238.2001
Copyright © 2001, American Society for Microbiology. All rights reserved.

hnRNP F Influences Binding of a 64-Kilodalton Subunit of Cleavage Stimulation Factor to mRNA Precursors in Mouse B Cells

Kristen L. Veraldi,¹ George K. Arhin,² Kathleen Martincic,¹ Ling-Hsiu Chung-Ganster,¹ Jeffrey Wilusz,² and Christine Milcarek¹^,^*

Department of Molecular Genetics and Biochemistry, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania 15261,¹ and Department of Microbiology and Molecular Genetics, UMDNJ-NJ Medical School, Newark, New Jersey 07103²

Received 31 May 2000/Returned for modification 7 July 2000/Accepted 16 November 2000

Previous studies on the regulation of polyadenylation of the immunoglobulin (Ig) heavy-chain pre-mRNA argued for trans-actingmodifiers of the cleavage-polyadenylation reaction operating differentiallyduring B-cell developmental stages. Using four complementary approaches,we demonstrate that a change in the level of hnRNP F is an importantdeterminant in the regulated use of alternative polyadenylationsites between memory and plasma stage B cells. First, by Westernanalyses of cellular proteins, the ratio of hnRNP F to H or H'was found to be higher in memory B cells than in plasma cells.In memory B cells the activity of CstF-64 binding to pre-mRNA,but not its amount, was reduced. Second, examination of the complexesformed on input pre-mRNA in nuclear extracts revealed large assemblagescontaining hnRNP H, H', and F but deficient in CstF-64 in memoryB-cell extracts but not in plasma cells. Formation of these largecomplexes is dependent on the region downstream of the AAUAAAin pre-mRNA, suggesting that CstF-64 and the hnRNPs compete fora similar region. Third, using a recombinant protein we showedthat hnRNP F could bind to the region downstream of a poly(A)site, block CstF-64 association with RNA, and inhibit the cleavagereaction. Fourth, overexpression of recombinant hnRNP F in plasmacells resulted in a decrease in the endogenous Ig heavy-chainmRNA secretory form-to-membrane ratio. These results demonstratethat mammalian hnRNP F can act as a negative regulator in thepre-mRNA cleavage reaction and that increased expression of Fin memory B cells contributes to the suppression of the Ig heavy-chainsecretory poly(A)site.

^* Corresponding author. Mailing address: Department of Molecular Genetics and Biochemistry and Graduate Program in Immunology,University of Pittsburgh School of Medicine, W1257 BiomedicalScience Tower, Pittsburgh, PA 15261. Phone: (412) 648-9098. Fax:(412) 624-1401. E-mail: milcarek{at}pitt.edu.

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