High mobility group proteins in ram spermatids.
The four major high mobility group proteins HMG 1, 2, 14 and 17, HMG 19B and histone H1(0) were identified in the ram testis by their extraction and solubility characteristics and by their electrophoretic mobilities. HMG 14 and 17 were isolated by chromatography and amino acid analysis revealed that they were similar to their calf thymus analogues. A protein, named 2R and co-extracted with HMG 14, was also purified and analysed. Electrophoretic analyses of the proteins extracted by 0.75 M perchloric acid (PCA) or by 0.35 M NaCl from round and non-round spermatids, separated by centrifugal elutriation, showed that the four major HMG proteins disappear from nuclei in the oldest round spermatids, at the time the nuclear content of protein 2R and histone H1(0) increases in spermatids. Ubiquitin and HMG 19B were present in the round and elongating spermatids, but not in elongated spermatids which contained only protamine. The relation was considered between several protein changes and genetic inactivation and structural reorganization of the spermatid chromatin.
D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002469:Cell Separation; D002843:Chromatin / Q000737:chemistry; D006609:High Mobility Group Proteins / Q000032:analysis*; D008297:Male; D012756:Sheep; D013087:Spermatids / Q000737:chemistry* / Q000166:cytology; D013737:Testis / Q000737:chemistry*
D000596:Amino Acids; D002843:Chromatin; D006609:High Mobility Group Proteins