Enzymatic phosphorylation of proteins of rat liver chromatin by (γ-32P) ATP in vitro

1971 ◽  
Vol 27 (1) ◽  
pp. 30-33 ◽  
Author(s):  
E. Schiltz ◽  
C. E. Sekeris
1977 ◽  
Vol 165 (2) ◽  
pp. 237-245 ◽  
Author(s):  
E Pays

At low ionic strength and with a low exogenous RNA polymerase/DNA ratio, rat liver chromatin directs the synthesis in vitro of RNA sequences rich in double-stranded segments. All the transcripts contain at least one double-stranded sequence. Most of the double-stranded segments are formed by intramolecular base-pairing of inverted complementary sequences separated by a single-stranded loop. They are heterogeneous in size, 35-45% of them being more than 80 nucleotides long. They contain 61-64% G+C, whether synthesized by rat liver RNA polymerase (form B) or Escherichia coli RNA polymerase. The largest double-stranded sequences are found in the largest transcripts, and are the most thermostable. The fidelity of base-matching is better in double-stranded transcripts synthesized on rat liver chromatin by homologous polymerase than in those synthesized on it by a bacterial polymerase, or in those synthesized by either of the two polymerases on pure DNA.


1984 ◽  
Vol 220 (1) ◽  
pp. 133-137 ◽  
Author(s):  
C Goffin ◽  
W G Verly

DNA from T7 phage containing AP (apurinic/apyrimidinic) sites was repaired by the successive actions of three chromatin enzymes [AP endodeoxyribonuclease, DNAase IV (5′----3′-exodeoxyribonuclease) and DNA polymerase-beta] prepared from rat liver and T4-phage DNA ligase. Since DNA ligase is also found in rat liver chromatin, all the activities used for the successful repair in vitro are thus present in the chromatin of a eukaryotic cell. Our results show, in particular, that the chromatin DNAase IV is capable of excising the AP site from the DNA strand nicked by the chromatin AP endodeoxyribonuclease. We did not try to combine all the enzymes, since competition between some of them might have prevented the repair; we have, for instance, shown that DNA ligase can seal the incision 5′ to the AP site made by the AP endodeoxyribonuclease. Changes in chromatin structure during repair might perhaps prevent this competition when nuclear DNA is repaired in the living cell.


1977 ◽  
Vol 68 (6) ◽  
pp. 413-415 ◽  
Author(s):  
GARY TALLMAN ◽  
DONALD BUTCHER ◽  
WALTER KACZMARCZYK ◽  
VALENTIN ULRICH
Keyword(s):  

Sign in / Sign up

Export Citation Format

Share Document