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PMID: 22001404 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Review

Tightly bound to DNA proteins: possible universal substrates for intranuclear processes.

Gene ·Vol. 492 ·No. 1 ·2012-01-15 ·Pages 54-64

Sjakste N, Bielskiene K, Bagdoniene L, Labeikyte D, Gutcaits A, Vassetzky Y, Sjakste T

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.

MeSH Terms
Animals Cell Nucleus/metabolism DNA-Binding Proteins/chemistry,metabolism Models, Biological Organ Specificity Phosphoric Monoester Hydrolases/metabolism Serpins/metabolism Species Specificity Transcription, Genetic
Chemicals
DNA-Binding Proteins Serpins Phosphoric Monoester Hydrolases
Authors & Affiliations
7 authors, click to expand affiliations / ORCID
Sjakste N
Faculty of Medicine, University of Latvia, Šarlotes 1a, LV1001, Riga, Latvia.
Bielskiene K
Bagdoniene L
Labeikyte D
Gutcaits A
Vassetzky Y
Sjakste T
Article Info
Journal
Gene
Abbr.
Gene
ISSN
1879-0038
Published
2012-01-15
Epub
2011-00-06
Pages
54-64
Language
English
Region
Netherlands
NLM ID
7706761
Subset
IM
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