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2006 | 53 | 3 | 507-513

Article title

On the possibility that H1 histone interaction with DNA occurs through phosphates connecting lysine and arginine side chain groups

Content

Title variants

Languages of publication

EN

Abstracts

EN
Gel filtration and velocity of sedimentation analyses on native and on lysine- and arginine- modified forms of the annelid worm Chaetopterus variopedatus sperm H1 histone indicate that anion-mediated lysine - arginine interactions play a relevant role in the stabilization of the oligomeric states of the molecule. CD spectroscopy shows that phosphate anions are at least an order of magnitude more efficient than chloride as negatively charged groups connecting H1 lysines and arginines. Acetylation of lysines, although not altering grossly the H1 properties, causes a tenfold decrease of the structuring efficiency of phosphates. This suggests that DNA phosphates may be sandwiched between lysine and arginine groups of H1 histone when this molecule binds to chromatin, constituting a relevant parameter for the reciprocal stabilization of the protein and of the chromatin higher order structures.

Year

Volume

53

Issue

3

Pages

507-513

Physical description

Dates

published
2006
received
2006-06-28
revised
2006-08-31
accepted
2006-09-07
(unknown)
2006-10-01

Contributors

  • Department of Structural and Functional Biology, Section of Genetic and Molecular Biology, University of Naples Federico II, Naples, Italy
  • CNR-Institute of Cybernetics "Eduardo Caianiello" Pozzuoli-Naples, Naples, Italy
  • Department of Structural and Functional Biology, Section of Genetic and Molecular Biology, University of Naples Federico II, Naples, Italy
  • Department of Structural and Functional Biology, Section of Genetic and Molecular Biology, University of Naples Federico II, Naples, Italy
  • Department of Biological Sciences, Section of Genetic and Molecular Biology; University of Naples Federico II, Naples, Italy

References

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Document Type

Publication order reference

Identifiers

YADDA identifier

bwmeta1.element.bwnjournal-article-abpv53p507kz
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