Abstract
Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10-15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.
| Original language | English |
|---|---|
| Pages (from-to) | 322-326 |
| Number of pages | 5 |
| Journal | FEBS Letters |
| Volume | 200 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 12 May 1986 |
| Externally published | Yes |
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Keywords
- Chromatin structure
- Flow linear dichroism
- Immobilized enzyme
- Light scattering
- Trypsin
ASJC Scopus subject areas
- Biochemistry
- Biophysics
- Molecular Biology
Cite this
Chromatin superstructure. A study with an immobilized trypsin. / Dimitrov, S. I.; Apostolova, T. M.; Makarov, V. L.; Pashev, I. G.
In: FEBS Letters, Vol. 200, No. 2, 12.05.1986, p. 322-326.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Chromatin superstructure. A study with an immobilized trypsin
AU - Dimitrov, S. I.
AU - Apostolova, T. M.
AU - Makarov, V. L.
AU - Pashev, I. G.
PY - 1986/5/12
Y1 - 1986/5/12
N2 - Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10-15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.
AB - Hen erythrocyte chromatin was treated with trypsin immobilized on collagen membranes and the unfolding of chromatin fiber was followed by light scattering at 90° and flow linear dichroism. Chromatin was found almost completely decondensed when the bulk of H1 and H5 was digested while H3 was still intact. Further digestion leading to degradation of both H3 and the rest of H1 and H5 accounted for no more than 10-15% of the total effect. When chromatin with trypsin-cleaved H1 and H5 was titrated with increasing amounts of spermidine it folded similarly to the control sample. This finding suggests that charge neutralization appears a likely mechanism for maintaining the structure of the 30 nm chromatin fiber by the C-terminal domain of H1 and H5.
KW - Chromatin structure
KW - Flow linear dichroism
KW - Immobilized enzyme
KW - Light scattering
KW - Trypsin
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UR - http://www.scopus.com/inward/citedby.url?scp=0022536182&partnerID=8YFLogxK
U2 - 10.1016/0014-5793(86)81161-9
DO - 10.1016/0014-5793(86)81161-9
M3 - Article
C2 - 3709797
AN - SCOPUS:0022536182
VL - 200
SP - 322
EP - 326
JO - FEBS Letters
JF - FEBS Letters
SN - 0014-5793
IS - 2
ER -