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The Plant Journal (1995) 7(2), 185-192 MINI-REVIEW eta/., 1990; Johns, 1982). It has been estimated that approximately one in every 10-15 nucleosomes, on aver- Klaus D. Grasser* age, might be associated with HMG1/2 and HMG14/17 Department of Biochemistry, University of Cambridge, (Johns, 1982). HMG proteins are subject to multiple Tennis Court Road, Cambridge CB2 1QW, UK post-translational modifications such as acetylation, methylation, phosphorylation, ADP-ribosylation and Introduction glycosylation, although the significance of these modifica- The high mobility group (HMG) proteins were originally tions is still unclear (van Holde, 1989). Despite their wide- discovered in the 1960s as contaminants in calf thymus spread occurrence, the biological function of these proteins histone H1 preparations (reviewed in Johns, 1982). They is still largely unknown, although there are numerous were operationally defined as small and abundant, 2% reports indicating an involvement in various cellular pro- cesses such as replication, transcription or nucleosome TCA-soluble non-histone proteins extractable from chro- assembly (reviewed by Bustin et al., 1990). matin with 0.35 M NaCI and having a high content of acidic and basic amino acid residues (Goodwin etaL, 1973). Therefore, according to this operational definition HMG proteins represent an artificial group of proteins that are Plant HMG proteins
The Plant Journal – Wiley
Published: Feb 1, 1995
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