Abstract
Limited digestion of nucleosome core particles with trypsin caused cleavage and removal of N‐terminal histone sequences of 10–30 amino acids. The proteolyzed core particles exhibited salt‐dependent structural transitions revealed by sedimentation, circular dichroism and nuclease‐cutting assays, while the intact nucleosome cores were not affected under the experimental conditions. The results obtained indicate that the observed transitions correspond to the transient unfolding of terminal segments of core particle nucleoprotein caused by the increase of its net negative charge. The excision of the N‐terminal histone domains therefore leads to partial destabilization but not to irreversible disruption of the compact nucleosome structure.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 119-125 |
| Number of pages | 7 |
| Journal | European Journal of Biochemistry |
| Volume | 129 |
| Issue number | 1 |
| DOIs | |
| State | Published - Dec 1982 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
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Transient Unfolding of Trypsin‐Digested Chromatin Core Particles. / GRIGORYEV, Sergei A.; KRASHENINNIKOV, Igor A.
In: European Journal of Biochemistry, Vol. 129, No. 1, 12.1982, p. 119-125.Research output: Contribution to journal › Article
TY - JOUR
T1 - Transient Unfolding of Trypsin‐Digested Chromatin Core Particles
AU - GRIGORYEV, Sergei A.
AU - KRASHENINNIKOV, Igor A.
PY - 1982/12
Y1 - 1982/12
N2 - Limited digestion of nucleosome core particles with trypsin caused cleavage and removal of N‐terminal histone sequences of 10–30 amino acids. The proteolyzed core particles exhibited salt‐dependent structural transitions revealed by sedimentation, circular dichroism and nuclease‐cutting assays, while the intact nucleosome cores were not affected under the experimental conditions. The results obtained indicate that the observed transitions correspond to the transient unfolding of terminal segments of core particle nucleoprotein caused by the increase of its net negative charge. The excision of the N‐terminal histone domains therefore leads to partial destabilization but not to irreversible disruption of the compact nucleosome structure.
AB - Limited digestion of nucleosome core particles with trypsin caused cleavage and removal of N‐terminal histone sequences of 10–30 amino acids. The proteolyzed core particles exhibited salt‐dependent structural transitions revealed by sedimentation, circular dichroism and nuclease‐cutting assays, while the intact nucleosome cores were not affected under the experimental conditions. The results obtained indicate that the observed transitions correspond to the transient unfolding of terminal segments of core particle nucleoprotein caused by the increase of its net negative charge. The excision of the N‐terminal histone domains therefore leads to partial destabilization but not to irreversible disruption of the compact nucleosome structure.
UR - http://www.scopus.com/inward/record.url?scp=0020390714&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0020390714&partnerID=8YFLogxK
U2 - 10.1111/j.1432-1033.1982.tb07029.x
DO - 10.1111/j.1432-1033.1982.tb07029.x
M3 - Article
C2 - 7160375
AN - SCOPUS:0020390714
VL - 129
SP - 119
EP - 125
JO - FEBS Journal
JF - FEBS Journal
SN - 1742-464X
IS - 1
ER -