Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
|
pubmed:dateCreated |
1995-12-14
|
pubmed:abstractText |
The primary structure of transition protein 4 (TP4) from boar late spermatid nuclei was determined by automated Edman degradation of S-pyridylethylated protein and of peptides generated by cleavage with Staphylococcus aureus V8 protease, lysyl endopeptidase and CNBr. Boar TP4 is a basic protein consisting of a highly basic amino-terminal half (residues 1-73) and a less basic carboxy-terminal half (residues 74-138). The latter half includes a highly hydrophobic segment, a four-times tandemly repeated sequence, N(G)QNKR(K)X, and a carboxy-terminal segment containing Trp126. Ultraviolet absorption and CD spectra of TP4-rat-liver-nucleosome-core-DNA (double-stranded DNA) complexes suggest a TP4-induced local melting of DNA. Although at 1 mM NaCl TP4 brought about a slight stabilization of the DNA against thermal melting, a destabilization of the DNA was observed at 50 mM NaCl. From the results of quenching of tryptophan (Trp126) fluorescence of TP4 upon its binding to double-stranded and single-stranded boar liver nucleosome-core DNA at 50 mM NaCl, the apparent association constants for the binding of TP4 to double-stranded and single-stranded DNA were calculated to be 7.3 x 10(3) M-1 and 4.1 x 10(3) M-1, respectively. These results suggest that TP4, having different domain structures from TP1-3 and a higher affinity for double-stranded DNA, induces a local destabilization of DNA probably through the stacking of Trp126 with nucleic acid bases.
|
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical | |
pubmed:status |
MEDLINE
|
pubmed:month |
Oct
|
pubmed:issn |
0014-2956
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:day |
1
|
pubmed:volume |
233
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
179-85
|
pubmed:dateRevised |
2007-7-23
|
pubmed:meshHeading |
pubmed-meshheading:7588743-Amino Acid Sequence,
pubmed-meshheading:7588743-Animals,
pubmed-meshheading:7588743-Chromosomal Proteins, Non-Histone,
pubmed-meshheading:7588743-Circular Dichroism,
pubmed-meshheading:7588743-DNA,
pubmed-meshheading:7588743-Male,
pubmed-meshheading:7588743-Molecular Sequence Data,
pubmed-meshheading:7588743-Molecular Structure,
pubmed-meshheading:7588743-Nucleic Acid Denaturation,
pubmed-meshheading:7588743-Nucleosomes,
pubmed-meshheading:7588743-Protein Binding,
pubmed-meshheading:7588743-Rats,
pubmed-meshheading:7588743-Repetitive Sequences, Nucleic Acid,
pubmed-meshheading:7588743-Spectrometry, Fluorescence,
pubmed-meshheading:7588743-Spectrophotometry, Ultraviolet,
pubmed-meshheading:7588743-Spermatids,
pubmed-meshheading:7588743-Swine
|
pubmed:year |
1995
|
pubmed:articleTitle |
The amino acid sequence and interaction with the nucleosome core DNA of transition protein 4 from boar late spermatid nuclei.
|
pubmed:affiliation |
Department of Chemistry, Faculty of Science, Chiba University, Japan.
|
pubmed:publicationType |
Journal Article,
In Vitro
|