Nuclear transition protein 2 (TP2) of mammalian spermatids has a very basic carboxyl terminal domain.
Nuclear transition protein 2 (TP2) along with TP1 are major basic chromosomal proteins of rat spermatids during the period of transition from histone-associated to protamine-associated DNA. TP2 isolated by reversed phase high pressure liquid chromatography was cleaved with S. aureus V8 protease to yield two fragments. The complete amino acid sequence of the 27 residue peptide assigned to the carboxyl terminus was established. It contains most of the basic residues of the protein and is likely to be a major site of DNA binding. Thus, TP2 is differentiated from core histones in having its basic domain at the carboxyl rather than amino terminal end.
Cole
K D
KD
Kistler
W S
WS
D000595:Amino Acid Sequence; D000596:Amino Acids / Q000032:analysis; D000818:Animals; D002467:Cell Nucleus / Q000032:analysis; D002843:Chromatin / Q000032:analysis; D002851:Chromatography, High Pressure Liquid; D002868:Chromosomal Proteins, Non-Histone / Q000032:analysis*; D010450:Endopeptidases / Q000378:metabolism; D008297:Male; D051381:Rats; D012697:Serine Endopeptidases; D013087:Spermatids / Q000032:analysis*; D013091:Spermatogenesis
D000596:Amino Acids; D002843:Chromatin; D002868:Chromosomal Proteins, Non-Histone; D010450:Endopeptidases; D012697:Serine Endopeptidases; C028344:glutamyl endopeptidase