PMID- 23581988
OWN - NLM
STAT- MEDLINE
DCOM- 20130930
LR  - 20130415
IS  - 1608-3040 (Electronic)
IS  - 0006-2979 (Linking)
VI  - 78
IP  - 2
DP  - 2013 Feb
TI  - Influence of chromatin structure, antibiotics, and endogenous histone methylation 
      on phosphorylation of histones H1 and H3 in the presence of protein kinase A in 
      rat liver nuclei in vitro.
PG  - 176-84
LID - 10.1134/S0006297913020065 [doi]
AB  - In vitro phosphorylation of histones H1 and H3 by cAMP-dependent protein kinase A 
      and endogenous phosphokinases in the presence of [gamma-(3)(2)P]ATP was studied in 
      isolated rat liver nuclei with different variants of chromatin structural 
      organization: condensed (diameter of fibrils 100-200 nm; N-1) and partly 
      decondensed (diameter of fibrils ~30 nm; N-2). In the N-1 state histone, H1 is 
      phosphorylated approximately twice as much than histone H3. Upon the 
      decondensation of the chromatin in the N-2 state, 1.5-fold decrease of total 
      phosphorylation of H1 is observed, while that of H3 does not change, although the 
      endogenous phosphorylation of both histones is reduced by half. Changes in 
      histone phosphorylation in the presence of low or high concentrations of 
      distamycin and chromomycin differ for H1 and H3 in N-1 and N-2. It was found that 
      distamycin (DM) stimulates the phosphorylation of tightly bound H1 fraction, 
      which is not extractable by polyglutamic acid (PG), especially in N-1. 
      Chromomycin (CM) increases the phosphorylation of both histones in PG extracts 
      and in the nuclear pellets, particularly in N-2. At the same time, in N-1 one can 
      detect phosphorylation of a tightly bound fraction of histones H1 whose N-termini 
      are located on AT-rich sites that become inaccessible for protein kinase in the 
      process of chromatin decondensation in N-2. At the same time, in N-2 the 
      accessibility for protein kinase A of tightly bound H1 fractions, whose N-termini 
      are located on GC-rich sites, increases dramatically. High concentrations of both 
      CM and DM in N-1 and N-2 stimulated phosphorylation of the non-extractable by PG 
      fraction of H1 whose N-termini are located on sites where AT  approximately  GC. CM at high 
      concentration stimulated 4-7 times the phosphorylation of a small fraction of H3, 
      which is extracted by PG from both types of nuclei. We detected an effect of 
      endogenous methylation of histones H1 and H3 in the nuclei on their subsequent 
      phosphorylation depending on the chromatin structure, histone-chromatin binding 
      strength, and concentration of DM.
FAU - Prusov, A N
AU  - Prusov AN
AD  - Belozersky Institute of Physico-Chemical Biology, Lomonosov Moscow State 
      University, 119991 Moscow, Russia. prusov@belozersky.msu.ru
FAU - Smirnova, T A
AU  - Smirnova TA
FAU - Kolomijtseva, G Ya
AU  - Kolomijtseva GY
LA  - eng
PT  - Journal Article
PL  - United States
TA  - Biochemistry (Mosc)
JT  - Biochemistry. Biokhimiia
JID - 0376536
RN  - 0 (Anti-Bacterial Agents)
RN  - 0 (Chromatin)
RN  - 0 (Histones)
RN  - EC 2.7.11.11 (Cyclic AMP-Dependent Protein Kinases)
SB  - IM
MH  - Animals
MH  - Anti-Bacterial Agents/*pharmacology
MH  - Cell Nucleus/chemistry/*drug effects/enzymology/ultrastructure
MH  - Chromatin/*chemistry
MH  - Cyclic AMP-Dependent Protein Kinases/*pharmacology
MH  - Histones/*metabolism
MH  - Liver/chemistry/*drug effects/enzymology/ultrastructure
MH  - Methylation/drug effects
MH  - Phosphorylation/drug effects
MH  - Rats
EDAT- 2013/04/16 06:00
MHDA- 2013/10/01 06:00
CRDT- 2013/04/16 06:00
PHST- 2013/04/16 06:00 [entrez]
PHST- 2013/04/16 06:00 [pubmed]
PHST- 2013/10/01 06:00 [medline]
AID - BCM78020243 [pii]
AID - 10.1134/S0006297913020065 [doi]
PST - ppublish
SO  - Biochemistry (Mosc). 2013 Feb;78(2):176-84. doi: 10.1134/S0006297913020065.