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Originally published In Press as doi:10.1074/jbc.M101692200 on May 16, 2001

J. Biol. Chem., Vol. 276, Issue 28, 25959-25969, July 13, 2001
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HMGN3a and HMGN3b, Two Protein Isoforms with a Tissue-specific Expression Pattern, Expand the Cellular Repertoire of Nucleosome-binding Proteins*

Katherine L. WestDagger §, Yuko ItoDagger , Yehudit Birger, Yuri Postnikov, Hitoshi Shirakawa, and Michael Bustin

From the Protein Section, Laboratory of Metabolism, Division of Basic Science, NCI, National Institutes of Health, Bethesda, Maryland 20892

HMGN1 (HMG-14) and HMGN2 (HMG-17) are nuclear proteins that bind specifically to nucleosomes, reduce the compactness of the chromatin fiber, and enhance transcription from chromatin templates. Here we report that many vertebrates contain an additional type of HMGN protein named HMGN3 (Trip 7). The human HMGN3 gene is located on chromosome 6 and spans 32 kilobase pairs, which is nearly 10-fold longer than the closely related HMGN2 gene. However, the intron/exon boundaries of the HMGN3 gene are identical to those of HMGN1 and HMGN2. Unique within the HMGN family, the HMGN3 transcript undergoes alternative splicing and generates two different variants, HMGN3a and HMGN3b. The shorter variant, HMGN3b, arises from an additional splice site that truncates exon V and causes a frameshift. The resulting HMGN3b protein lacks the majority of the C-terminal chromatin-unfolding domain. Both splice variants are found in many vertebrates from frogs to man and are expressed in many tissues. The pattern of tissue-specific expression differs considerably from those of HMGN1 and HMGN2 at both the mRNA and the protein level. Our results expand the multiplicity of the HMGN protein family and raise the possibility that these nucleosome-binding proteins function as co-activators in tissue-specific gene expression.

* 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.

Dagger Both authors contributed equally to this work.

§ To whom correspondence and reprint requests should be addressed: Bldg. 37, Rm. 3D12, NCI, National Institutes of Health, Bethesda, MD 20892. Tel.: 301-496-5235; E-mail: klmarsh@pop.nci.nih.gov.

Present address: Laboratory of Nutrition, Division of Life Sciences, Graduate School of Agricultural Science, Tohoku University, 1-1 Tsutsumidori-Amamiya-cyo, Aoba-ku, Sendai 981-8555, Japan.

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