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Originally published In Press as doi:10.1074/jbc.M110023200 on December 13, 2001

J. Biol. Chem., Vol. 277, Issue 9, 7598-7609, March 1, 2002
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Characterization of Two Novel Nuclear BTB/POZ Domain Zinc Finger Isoforms
ASSOCIATION WITH DIFFERENTIATION OF HIPPOCAMPAL NEURONS, CEREBELLAR GRANULE CELLS, AND MACROGLIA*

Cathy Mitchelmore, Karen M. Kjærulff, Hans C. Pedersen, Jakob V. Nielsen, Thomas E. Rasmussen, Mads F. Fisker, Bente FinsenDagger , Karen M. Pedersen, and Niels A. Jensen§

From the Laboratory of Mammalian Molecular Genetics, The Panum Institute 6.5, University of Copenhagen, Blegdamsvej 3, DK-2200 Copenhagen N and the Dagger  Department of Anatomy and Neurobiology, University of Odense, Winsløwparken 21, DK-5000 Odense C, Denmark

BTB/POZ (broad complex tramtrack bric-a-brac/poxvirus and zinc finger) zinc finger factors are a class of nuclear DNA-binding proteins involved in development, chromatin remodeling, and cancer. However, BTB/POZ domain zinc finger factors linked to development of the mammalian cerebral cortex, cerebellum, and macroglia have not been described previously. We report here the isolation and characterization of two novel nuclear BTB/POZ domain zinc finger isoforms, designated HOFL and HOFS, that are specifically expressed in early hippocampal neurons, cerebellar granule cells, and gliogenic progenitors as well as in differentiated glia. During embryonic development of the murine cerebral cortex, HOF expression is restricted to the hippocampal subdivision. Expression coincides with early differentiation of presumptive CA1 and CA3 pyramidal neurons and dentate gyrus granule cells, with a sharp decline in expression at the CA1/subicular border. By using bromodeoxyuridine labeling and immunohistochemistry, we show that HOF expression coincides with immature non-dividing cells and is down-regulated in differentiated cells, suggesting a role for HOF in hippocampal neurogenesis. Consistent with the postulated role of the POZ domain as a site for protein-protein interactions, both HOF isoforms are able to dimerize. The HOF zinc fingers bind specifically to the binding site for the related promyelocytic leukemia zinc finger protein as well as to a newly identified DNA sequence.

* This work was supported by grants from the Lundbeck Foundation, the Danish Cancer Society, Løvens Kemiske Fabriks Foundation, the Michelsen Foundation, and the NOVO-Nordisk Foundation.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/EBI Data Bank with accession number(s) AF185576 and AF194030.

§ To whom correspondence should be addressed. Tel.: 45-35327722; Fax: 45-35327701; E-mail: naj@imbg.ku.dk.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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