Interaction of rat testis protein, TP, with nucleosome core particle.
Circular dichroism studies have revealed that addition of testis specific protein, TP in vitro, to rat testes nucleosome core particle resulted in a decrease in the compaction of the core particle DNA. This was also corroborated by thermal denaturation analysis. Addition of TP to nucleosome core particle resulted in the conversion of a biphasic transition towards a single phase. However, at the same time there was a 20% reduction in the overall hyperchromicity of core particle DNA at core particle to TP molar ratios of 1:2 and 1:3. These observations along with our earlier report, showing the DNA melting properties of TP, suggest that TP may play an important role in the disassembly process of nucleosome core particle during spermiogenesis.
Singh
J
J
Department of Biochemistry, Indian Institute of Science, Bangalore.
Rao
M R
MR
D000818:Animals; D002942:Circular Dichroism; D004247:DNA / Q000378:metabolism*; D047908:Intracellular Signaling Peptides and Proteins; D008297:Male; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins / Q000378:metabolism*; D009691:Nucleic Acid Denaturation; D009707:Nucleosomes / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013737:Testis / Q000378:metabolism*; D044767:Ubiquitin-Protein Ligases; D056427:t-Complex Genome Region
D047908:Intracellular Signaling Peptides and Proteins; D008869:Microtubule-Associated Proteins; D009687:Nuclear Proteins; D009707:Nucleosomes; D004247:DNA; C116196:PPP1R11 protein, human; D044767:Ubiquitin-Protein Ligases