ADP ribosylation of rat liver nucleosomal core histones.

L. O. Burzio, P. T. Riquelme, S. S. Koide

Resultado de la investigación: Contribución a una revistaArtículorevisión exhaustiva

125 Citas (Scopus)


When nucleosomal core histones were isolated from rat liver nuclei incubated with [14C]NAD+ and fractionated into the individual components (H2A, H2B, H3, and H4), [14C]adenosine diphosphate ribose (ADP-Rib) was found to be associated with all of them. However, while about 15% of the H2B molecules were modified, less than 2% of the other fractions contained radioactive ADP-Rib. The nucleotide attached to H2B was identified as a single monomer of ADP-Rib. On subjectint H2B to electrophoresis in polyacrylamide gels containing 2.5 M urea and 0.9 N acetic acid, one single band of H2B with 5% less mobility than the unomdified control was obtained. The linkage between H2B and ADP-Rib was rapidly hydrolyzed with 0.1 N NaOH or with 1 M neutral hydroxylamine. Hydrolysis of ADP-ribosylated H2B with trypsin generated a single peptide linked to ADP-Rib, which corresponded to the sequence Pro-Glu-Pro-Ala-Lys. We were able to dansylate the NH2-terminal proline, which proved that the imino group of this amino acid was not substituted. These findings, together with the chemical properties of the linkage, which were typical of those of an ester-like bond, strongly suggest that the ADP-Rib residue was linked to the gamma-COOH group of the glutamic acid in position 2 of H2B.

Idioma originalInglés
Páginas (desde-hasta)3029-3037
Número de páginas9
PublicaciónJournal of Biological Chemistry
EstadoPublicada - 25 abr. 1979

Áreas temáticas de ASJC Scopus

  • Bioquímica
  • Biología molecular
  • Biología celular


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