The occurrence of extended acidic sequences in nonhistone chromosomal proteins.
Nonhistone chromosomal proteins and soluble cytoplasmic proteins from rat liver were treated with a combination of proteases and chemical reagents which split a variety of peptide bonds but do not attack sequences consisting predominantly or exclusively of acidic amino acid residues. Analysis of the resulting digests by gel filtration chromatography and column electrophoresis demonstrated that, relative to cytoplasmic proteins, nonhistone chromosomal proteins are rich in highly charged, acidic peptides up to 12 residues in length, but rarely contain very long peptides consisting exclusively of acidic residues such as are found in the nonhistone chromosomal proteins HMG1 and HMG2.
Kuehl
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Childers
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McCauley
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D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001224:Aspartic Acid; D002467:Cell Nucleus / Q000032:analysis*; D002850:Chromatography, Gel; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis*; D003593:Cytoplasm / Q000032:analysis; D005971:Glutamates; D018698:Glutamic Acid; D008099:Liver / Q000032:analysis*; D008297:Male; D008970:Molecular Weight; D010446:Peptide Fragments / Q000032:analysis; D010447:Peptide Hydrolases; D051381:Rats
D000596:Amino Acids; D002868:Chromosomal Proteins, Non-Histone; D005971:Glutamates; D010446:Peptide Fragments; D001224:Aspartic Acid; D018698:Glutamic Acid; D010447:Peptide Hydrolases