caa a22 4500 39755835X CHVBK 20180308164809.0 cr unu---uuuuu 161202e199603 xx s 000 0 eng 10.1093/oxfordjournals.jbchem.a021262 doi (NATIONALLICENCE)oxford-10.1093/oxfordjournals.jbchem.a021262 Interaction of Nucleosome Core DNA with Transition Proteins 1 and 3 from Boar Late Spermatid Nuclei [Elektronische Daten] [Kuniko Akama, Hiroki Sato, Miki Furihata-Yamauchi, Yasuhiko Komatsu, Tohru Tobita, Minoru Nakano] The DNA binding properties of boar transition proteins 1 and 3 (TP1 and TP3) were studied by means of physicochemical techniques. The ultraviolet difference absorption spectra upon TP1 and TP3 binding to rat liver nucleosome core DNA (double-stranded DNA) showed TP1- and TP3-induced hyperchromicity at 260 nm, which is suggestive of local melting of DNA. CD measurements of TP1-DNA and TP3-DNA complexes indicated that the binding of TP1 and TP3 induced different conformational changes in DNA, probably including local melting of DNA. Thermal melting studies on the binding of TP1 and TP3 to DNA showed that although at 1 mM NaCl TP1 and TP3 caused slight stabilization of the DNA against thermal melting, destabilization of the DNA was observed at 50 mM NaCl. From the results of quenching of the tyrosine fluorescence of TP1 and the tryptophan fluorescence of TP3 upon their binding to double-stranded and single-stranded boar liver nucleosome core DNA at 50 mM NaCl, the apparent association constants for the binding of TP1 to double- and single-stranded DNA were calculated to be 8.0×10−4 and 1.3×105M−1, respectively, and those for the binding of TP3 to double- and single-stranded DNA to be 7.1×104 and 1.8×105 M−1, respectively. These results suggest that TP1 and TP3, having higher affinity for single-stranded DNA, induce local destabilization of DNA, probably through the stacking of Tyr32 and Trpl8 with nucleic acid bases, respectively. © by the Journal of Biochemistry Regular Papers nationallicence DNA-protein interaction nationallicence late spermatid nuclei nationallicence transition protein nationallicence Akama Kuniko Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut Sato Hiroki Graduate School of Science and Technology, Chiba University Chiba, Chiba 263 aut Furihata-Yamauchi Miki Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut Komatsu Yasuhiko National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology 1-1 Higashi, Tsukuba, Ibaraki 305 aut Tobita Tohru Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut Nakano Minoru Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut The Journal of Biochemistry Oxford University Press 119/3(1996-03), 448-455 0021-924X 119:3<448 1996 119 jbchem https://doi.org/10.1093/oxfordjournals.jbchem.a021262 text/html Onlinezugriff via DOI 1 research-article jats NATIONALLICENCE 856 40 https://doi.org/10.1093/oxfordjournals.jbchem.a021262 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Akama Kuniko Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut NATIONALLICENCE 700 1- Sato Hiroki Graduate School of Science and Technology, Chiba University Chiba, Chiba 263 aut NATIONALLICENCE 700 1- Furihata-Yamauchi Miki Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut NATIONALLICENCE 700 1- Komatsu Yasuhiko National Institute of Bioscience and Human Technology, Agency of Industrial Science and Technology 1-1 Higashi, Tsukuba, Ibaraki 305 aut NATIONALLICENCE 700 1- Tobita Tohru Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut NATIONALLICENCE 700 1- Nakano Minoru Department of Chemistry, Faculty of Science, Chiba University Chiba, Chiba 263 aut NATIONALLICENCE 773 0- The Journal of Biochemistry Oxford University Press 119/3(1996-03), 448-455 0021-924X 119:3<448 1996 119 jbchem Metadata rights reserved CC BY-NC-4.0 http://creativecommons.org/licenses/by-nc/4.0 nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-oxford