Tightly bound to DNA proteins: possible universal substrates for intranuclear processes |
| |
Authors: | Sjakste N Bielskiene K Bagdoniene L Labeikyte D Gutcaits A Vassetzky Y Sjakste T |
| |
Affiliation: | a Faculty of Medicine, University of Latvia, Šarlotes 1a, LV1001, Riga, Latviab Latvian Institute of Organic Synthesis, Aizkraukles 21, Riga, LV 1006, Latviac Laboratory of Molecular Oncology, Institute of Oncology, Vilnius University, P. Baublio Street 36, LT-08406, Vilnius, Lithuaniad Department of Biochemistry and Biophysics, Vilnius University, M. K. ?iurlionio 21, LT2009 Vilnius, Lithuaniae UMR-8126, Institut Gustave Roussy, 39, rue Camille-Desmoulins, 94805 Villejuif, Francef Genomics and Bioinformatics, Institute of Biology, University of Latvia, Miera 3, LV2169 Salaspils, Latvia |
| |
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. |
| |
Keywords: | TBPs, tightly bound to DNA proteins HMG, high mobility group proteins DNPs, DNA-protein complexes MENT, myeloid and erythroid nuclear termination stage specific protein MALDI TOF-MS, Matrix Asisted Laser Desorbtion/Ionization Time of Flight Mass spectrometry BAF, barrier to autointegration factor MAR, matrix attachment region PK, protein kinase |
本文献已被 ScienceDirect PubMed 等数据库收录! |
|