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Tightly bound to DNA proteins: Possible universal substrates for intranuclear processes

  • N. Sjakste
  • , K. Bielskiene
  • , L. Bagdoniene*
  • , D. Labeikyte
  • , A. Gutcaits
  • , Y. Vassetzky
  • , T. Sjakste
  • *Corresponding author for this work
  • Latvian Institute of Organic Synthesis
  • Vilnius University
  • Gustave Roussy-Cancer Campus

Research output: Contribution to journalReview articlepeer-review

5 Citations (Scopus)

Abstract

Tightly bound to DNA proteins (TBPs) are a protein group that remains attached to DNA after its deproteinization by phenol, chloroform or salting-out. TBP are bound to DNA with covalent phosphotriester or non-covalent ion and hydrogen bonds. They appear to be a vast protein group involved in numerous intranuclear processes. The TBPs fraction co-purified with DNA deproteinized by mild procedures is extremely heterogeneous, tissue and species-specific. The protein fraction co-purified with DNA after harsh deproteinization procedures appears to be formed from few polypeptides common to different species and tissues. Interaction sites between DNA and TBPs depend on the physiological status of the cell. The binding sites of TBPs to DNA do not co-localize with the nuclear matrix attachment regions. We hypothesize that TBPs form a universal substrate for intranuclear processes.

Original languageEnglish
Pages (from-to)54-64
Number of pages11
JournalGene
Volume492
Issue number1
DOIs
Publication statusPublished - 15 Jan 2012

OECD Field of Science

  • 3. Medical and Health Sciences

Keywords

  • Differentiation
  • DNA-proteins interaction
  • Nuclear matrix
  • Phosphatases
  • Serpins
  • Transcription

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