z-logo
open-access-imgOpen Access
ADP‐Ribosylated Histone H1 from HeLa Cultures
Author(s) -
ADAMIETZ Peter,
BREDEHORST Reinhard,
HILZ Helmuth
Publication year - 1978
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1978.tb12682.x
Subject(s) - histone h1 , histone , hela , ribose , nad+ kinase , biochemistry , adp ribosylation , chemistry , microbiology and biotechnology , in vitro , biology , enzyme , dna
ADP‐ribosylated histone H1 was isolated from intact HeLa cells grown for 24 h with [ 3 H]‐adenosine and compared with ADP‐ribosylated histone H1 synthesized from [ 3 H]NAD by isolated HeLa nuclei. Most (ADP‐ribose) n ‐histone H1 conjugates formed in vivo carried single ADP‐ribose units, less than one fourth of the total ADP‐ribose residues being in the form of oligomeric or polymeric chains. (ADP‐ribose) n linked to H1 in vivo was not released by neutral NH 2 OH to a significant extent. Alkali treatment (pH 10.5) liberated most but not all of the ADP‐ribose residues which may indicate the existence of a new type of linkage so far found only in conjugates isolated from intact tissue. No ADP‐ribosylated histone H1 complex of higher molecular weight (‘H1 dimer’) could be detected in intact cells. By contrast, isolated HeLa nuclei formed ADP‐ribosylated histone H1 which contained predominantly polymeric ADP‐ribose residues. The (ADP‐ribose) n residues were linked by NH 2 OH‐sensitive and by NH 2 OH‐resistant, alkali (pH 10.5) labile bonds, the majority of the conjugates appearing in the form of the higher‐molecular‐weight complex. A comparison with the ADP‐ribosylated non‐histone proteins indicated that histone H1 formed in vivo carried less than 2.5% of the total protein‐bound ADP‐ribose residues and less than 1% of the protein‐bound ADP‐ribose synthesized in vitro .

The content you want is available to Zendy users.

Already have an account? Click here to sign in.
Having issues? You can contact us here