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M Bustin

Publications and source records attributed to M Bustin.

178 records · Page 10Linked to original sources

Nitration of the tyrosine in histone F1 in salt solutions and in F1-polyanion complexes.

The reaction of histone F1 with tetranitromethane was used to study the environment of the single tyrosine residue in the molecule. It was found that at a 10-fold molar excess of tetranitromethane over tyrosine approx. 40 min were needed to convert 85% of the tyrosine residues to nitrotyrosine. The rate and extent of nitration of F1 in dilute salt solutions was used as a reference against which the rate and extent of nitration under conditions known to affect the conformation of F1 was measured. In 1.0 M NaCl solutions the rate of nitration decreased, suggesting that the presence of salt may cause a conformational change in the tyrosine containing region of the histone. When the histone is complexed with polyanions such as DNA, RNA or poly-L-glutamic acid the accessibility of the tyrosine to nitration is markedly reduced. The results indicate that upon association with polyanions the non-cationic, tyrosine-containing, region in F1 undergoes a conformational change or alternatively, this tyrosine containing region is tightly associated with the polyanion.

Animals↗

Histone structure: asymmetric distribution of lysine residues in lysine-rich histone.

Structural studies on a very lysine-rich histone show that the carboxyl-terminal half of the molecule is enriched in lysine (and proline). which suggests that it is a site for binding to DNA. The amino-terminal half. containing most of the acidic residues. resembles small, nonhistone proteins and so might have specificity for factors other than DNA.

Amino Acid Sequence↗