Structure and Function in the HMG-1 Family of Chromosomal Proteins

  • Pere Puigdomènech
  • Matilde Jose
Part of the NATO ASI Series book series (NSSA, volume 101)


Analysis of HMG chromosomal proteins by SDS-polyacrylamide gel electrophoresis reveals a group of polypeptides in the region around 26,000 daltons. These are the proteins of the high mobility group that have the lowest electrophoretic mobility in both SDS and acid/urea gels and they have therefore been called HMG-1 or 2 in most tissues. For historical reasons, homologous proteins from trout testis and chicken erythrocytes are called HMG-T and HMG-E, respectively. In the rest of the present article HMG-1, 2, T, or E are considered to comprise the HMG-1 family. Apart from their apparent molecular weights, all these proteins share many common structural features, as can be expected from their similar amino acid compositions and sequences. In fact, the information that we have about the proteins of the HMG-1 family is mostly structural. Very little functional information is available and most of it is inferred from in vitro studies. In this respect, the situation of our knowledge on the HMG-1 family of proteins is very different than that for HMG-14 and 17. In the case of the latter, low molecular weight HMG proteins, there is considerable literature on their possible function, although firm conclusions are not yet available (see chapter by Goodwin et al., this volume). The low molecular weight HMG proteins do not display any evidence of secondary or tertiary folding. For the HMG-1 family the most interesting results have, in contrast, been in structural studies of the proteins and studies on their interactions with other macromolecules.


High Mobility Group Chromosomal Protein Chicken Erythrocyte Micrococcal Nuclease High Mobility Group Protein 
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Copyright information

© Plenum Press, New York 1985

Authors and Affiliations

  • Pere Puigdomènech
    • 1
  • Matilde Jose
    • 1
  1. 1.Institut de Biologia de Barcelona del CSICBarcelonaSpain

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