Chromatin superstructure

Nature ◽  
1976 ◽  
Vol 262 (5569) ◽  
pp. 533-533 ◽  
Author(s):  
H. G. Davies
Keyword(s):  
Chromatin Superstructure

scholarly journals Resistance of chromatin superstructure to tryptic digestion modulated by conjugated polyacrylamide

FEBS Letters ◽  
1983 ◽  
Vol 157 (1) ◽  
pp. 111-114 ◽  
Author(s):  
G.T.P. Saccone ◽  
J.D. Skinner ◽  
L.A. Burgoyne
Keyword(s):  
Tryptic Digestion ◽  
Chromatin Superstructure

TRYPTIC DIGESTION AS A PROBE TO STUDY CHROMATIN SUPERSTRUCTURE

1981 ◽  
Vol 9 (2) ◽  
pp. 124P-124P
Author(s):  
R. M. Nieto-Sandoval ◽  
L. Franco
Keyword(s):  
Tryptic Digestion ◽  
Chromatin Superstructure

scholarly journals Modulation of chromatin superstructure induced by poly(ADP-ribose) synthesis and degradation.

1986 ◽  
Vol 261 (15) ◽  
pp. 7011-7017
Author(s):  
G de Murcia ◽  
A Huletsky ◽  
D Lamarre ◽  
A Gaudreau ◽  
J Pouyet ◽  
...  
Keyword(s):  
Chromatin Superstructure ◽  
Synthesis And Degradation

Review: Modulation of chromatin structure by poly(ADP-ribosyl)ation

1988 ◽  
Vol 66 (6) ◽  
pp. 626-635 ◽  
Author(s):  
G. de Murcia ◽  
A. Huletsky ◽  
G. G. Poirier
Keyword(s):  
Dna Repair ◽  
Excision Repair ◽  
Histone H1 ◽  
Histone H2b ◽  
Repair Enzymes ◽  
Core Histones ◽  
Partial Dissociation ◽  
Chromatin Superstructure

Poly(ADP–ribose) polymerase is a nuclear enzyme that is highly conserved in eucaryotes. Its activity is totally dependent on the presence of DNA containing single or double stranded breaks. We have shown that this activation results in a decondensation of chromatin superstructure in vitro, which is caused mainly by hyper(ADP-ribosyl)ation of histone H1. In core particles, the modification of histone H2B leads to a partial dissociation of DNA from core histones. The conformational change of native chromatin by poly(ADP-ribosyl)ation is reversible upon degradation of the histone H1-bound poly(ADP–ribose) by poly(ADP–ribose) glycohydrolase. We propose that cuts produced in vivo on DNA during DNA repair activate poly(ADP–ribose) polymerase, which then synthesizes poly(ADP–ribose) on histone H1, in particular, and contributes to the opening of the 25-nm chromatin fiber, resulting in the increased accessibility of DNA to excision repair enzymes. This mechanism is fast and reversible.

Chromatin superstructure-dependent crosslinking with DNA of the histone H5 residues Thr1, His25 and His62

1990 ◽  
Vol 211 (2) ◽  
pp. 479-491 ◽  
Author(s):  
Andrei D. Mirzabekov ◽  
Dmitrii V. Pruss ◽  
Konstantin K. Ebralidse
Keyword(s):  
Histone H5 ◽  
Chromatin Superstructure

Chromatin superstructure

FEBS Letters ◽  
1986 ◽  
Vol 200 (2) ◽  
pp. 322-326 ◽  
Author(s):  
S.I. Dimitrov ◽  
T.M. Apostolova ◽  
V.L. Makarov ◽  
I.G. Pashev
Keyword(s):  
Chromatin Superstructure
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