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• W4239294804 endingPage "1923" @default.
• W4239294804 startingPage "1915" @default.
• W4239294804 abstract "We have identified, purified, and characterized a high-mobility-group (HMG) protein and its cDNAs from Drosophila melanogaster. This protein, HMG D, shares most of the characteristics of vertebrate HMG proteins; it is extractable from nuclei with 0.35 M NaCl, is soluble in 5% perchloric acid, is relatively small (molecular weight of 12,000), has both a high basic (24%) and high acidic (24%) amino acid content, and is a DNA-binding protein. HMG D exhibits characteristics of both the vertebrate HMG 1 and 2 class and the HMG 14 and 17 class of proteins. Its amino acid sequence is similar (36% amino acid identity) to that of HMG1, while its size and selective extraction with ethidium bromide are similar to properties of the HMG 14 and 17 class of proteins. HMG D is encoded by a single-copy gene that maps to 57F8-11 on the right arm of chromosome 2. Two transcripts are observed during embryogenesis; the protein is relatively stable throughout development. By the biochemical criteria of size, solubility, and amino acid content, HMG D appears to be the major HMG protein of D. melanogaster." @default.
• W4239294804 created "2022-05-12" @default.
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• W4239294804 date "1992-05-01" @default.
• W4239294804 modified "2023-09-26" @default.
• W4239294804 title "A High-Mobility-Group Protein and Its cDNAs from <i>Drosophila melanogaster</i>" @default.
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• W4239294804 doi "https://doi.org/10.1128/mcb.12.5.1915-1923.1992" @default.
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