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Ethidium bromide preferentially releases high mobility group chromosomal proteins HMGc and HMGd from wheat embryo nuclei
Author(s) -
Arwood Laura J.,
Hill Elizabeth,
Spiker Steven
Publication year - 1991
Publication title -
physiologia plantarum
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.351
H-Index - 146
eISSN - 1399-3054
pISSN - 0031-9317
DOI - 10.1111/j.1399-3054.1991.tb02927.x
Subject(s) - ethidium bromide , biology , chromatin , high mobility group , embryo , dna , bioassay , microbiology and biotechnology , non histone protein , genetics , dna binding protein , biochemistry , gene , transcription factor
The High Mobility Group (HMG) chromosomal proteins have been implicated as structural proteins of transcriptionally poised chromatin in animal systems. Despite the suspected functions of these proteins, no bioassay for them exists and they are defined operationally (by the procedures used to isolate and purify them). Plant systems have chromosomal proteins that can be operationally defined as HMG proteins. However, because of the lack of suitable bioassays and because the plant HMG proteins are structurally distinct from their putative animal counterparts, no clear relationship between plant and animal HMG proteins has been established. One diagnostic characteristic of vertebrate animal HMG proteins is that a subset of them is released from chromatin by intercalating agents that affect the topology of DNA. We show here that wheat ( Triticum aestivum ) embryo HMGc and HMGd (but not HMGa and HMGb) are preferentially released from nuclei treated with 7.5 m M ethidium bromide. Because vertebrate animal HMG14/17 (but not HMG1/2) displays this characteristic, the observation suggests that these wheat chromosomal proteins may be the plant analogs of vertebrate HMG14/17.