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Originally published In Press as doi:10.1074/jbc.M009307200 on April 6, 2001

J. Biol. Chem., Vol. 276, Issue 26, 23974-23985, June 29, 2001
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A New Spectrin, beta IV, Has a Major Truncated Isoform That Associates with Promyelocytic Leukemia Protein Nuclear Bodies and the Nuclear Matrix*

William T. TseDagger §, Ju TangDagger , Ou JinDagger , Catherine KorsgrenDagger , Kathryn M. JohnDagger , Andrew L. KungDagger , Babette Gwynn, Luanne L. Peters, and Samuel E. LuxDagger

From the Dagger  Division of Hematology/Oncology, Children's Hospital, and the Dana-Farber Cancer Institute, Harvard Medical School, Boston, Massachusetts 02115 and  The Jackson Laboratory, Bar Harbor, Maine 04609

We isolated cDNAs that encode a 77-kDa peptide similar to repeats 10-16 of beta -spectrins. Its gene localizes to human chromosome 19q13.13-q13.2 and mouse chromosome 7, at 7.5 centimorgans. A 289-kDa isoform, similar to full-length beta -spectrins, was partially assembled from sequences in the human genomic DNA data base and completely cloned and sequenced. RNA transcripts are seen predominantly in the brain, and Western analysis shows a major peptide that migrates as a 72-kDa band. This new gene, spectrin beta IV, thus encodes a full-length minor isoform (Spbeta IVSigma 1) and a truncated major isoform (Spbeta IVSigma 5). Immunostaining of cells shows a micropunctate pattern in the cytoplasm and nucleus. In mesenchymal stem cells, the staining concentrates at nuclear dots that stain positively for the promyelocytic leukemia protein (PML). Expression of Spbeta IVSigma 5 fused to green fluorescence protein in cells produces nuclear dots that include all PML bodies, which double in number in transfected cells. Deletion analysis shows that partial repeats 10 and 16 of Spbeta IVSigma 5 are necessary for nuclear dot formation. Immunostaining of whole-mount nuclear matrices reveals diffuse positivity with accentuation at PML bodies. Spectrin beta IV is the first beta -spectrin associated with a subnuclear structure and may be part of a nuclear scaffold to which gene regulatory machinery binds.

* This work is supported by National Institutes of Health Grants HL33262 and DK34083 (to S. E. L.) and HL55321 and HL64885 (to L. L. P.), by grants from the American Heart Association and the March of Dimes Birth Defects Foundation (to L. L. P.), by National Cancer Institute Grant CA34196 to the Jackson Laboratory, and by a fellowship from the Howard Hughes Medical Institute (to A. L. K.). The Children's Hospital Mental Retardation Research Center DNA Sequencing Core Facility is supported by Grant NIH-P30-HD18655.The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The nucleotide sequence(s) reported in this paper has been submitted to the GenBankTM/EMBL Data Bank with accession number(s) AF311855 and AF311856.

§ To whom correspondence should be addressed: Division of Hematology/Oncology, Children's Hospital, 300 Longwood Ave., Boston, MA 02115. Tel.: 617-355-7904; Fax: 617-355-7262; E-mail: william.tse@tch.harvard.edu.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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