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© The Rockefeller University Press, 0021-9525/1997//19 $5.00
The Journal of Cell Biology, Volume 137, Number 1, , 1997 19-26

Article

High Mobility Group 1 Protein Is Not Stably Associated with the Chromosomes of Somatic Cells



Luca Falciola*,{ddagger}, Fabio Spada*, Sabina Calogero{ddagger}, Gernot Längst§, Renate Voit§, Ingrid Grummt§, and Marco E. Bianchi*,{ddagger}

* Dipartimento di Genetica e di Biologia dei Microrganismi, Universitá di Milano, 20133 Milano, Italy; {ddagger} DIBIT, San Raffaele Scientific Institute, 20132 Milano, Italy; and § Deutsches Krebsforschungszentrum, 69120 Heidelberg, Germany

High mobility group 1 (HMG1) protein is an abundant and conserved component of vertebrate nuclei and has been proposed to play a structural role in chromatin organization, possibly similar to that of histone H1. However, a high abundance of HMG1 had also been reported in the cytoplasm and on the surface of mammalian cells. We conclusively show that HMG1 is a nuclear protein, since several different anti-HMG1 antibodies stain the nucleoplasm of cultured cells, and epitope-tagged HMG1 is localized in the nucleus only. The protein is excluded from nucleoli and is not associated to specific nuclear structures but rather appears to be uniformly distributed. HMG1 can bind in vitro to reconstituted core nucleosomes but is not stably associated to chromatin in live cells. At metaphase, HMG1 is detached from condensed chromosomes, contrary to histone H1. During interphase, HMG1 readily diffuses out of nuclei after permeabilization of the nuclear membranes with detergents, whereas histone H1 remains associated to chromatin. These properties exclude a shared function for HMG1 and H1 in differentiated cells, in spite of their similar biochemical properties. HMG1 may be stably associated only to a very minor population of nucleosomes or may interact transiently with nucleosomes during dynamic processes of chromatin remodeling.

Abbreviations used in this paper: HMG1, high mobility group 1 protein; LDH, lactate dehydrogenase.

Please address all correspondence to Marco Bianchi, DIBIT, via Olgettina 58, 4° piano A1, 20132 Milano, Italy. Tel.: 39-2-264-34780; Fax.: 39-2-26434767; E-mail: bianchm{at}dibit.hsr.it

L. Falciola's current address: Department de Biologie Moleculaire, 30 quai Ernest Ansermet, 1211 Geneve, Switzerland.


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