The nuclear matrix protein NMP-1 is the transcription factor YY1
| Autor: | B Guo, P R Odgren, A J van Wijnen, T J Last, J Nickerson, S Penman, J B Lian, J L Stein, G S Stein |
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| Rok vydání: | 1995 |
| Předmět: |
Blotting
Western Molecular Sequence Data Cross Reactions Biology Antibody Specificity medicine Animals Humans Nuclear Matrix Nuclear protein Scaffold/matrix attachment region Transcription factor YY1 Transcription Factor Nuclear receptor co-repressor 1 Cell Nucleus Regulation of gene expression Binding Sites Multidisciplinary Base Sequence YY1 DNA Nuclear matrix Molecular biology Recombinant Proteins Cell Compartmentation Rats DNA-Binding Proteins Cell nucleus medicine.anatomical_structure Oligodeoxyribonucleotides embryonic structures Erythroid-Specific DNA-Binding Factors Cell Nucleolus HeLa Cells Protein Binding Transcription Factors Research Article |
| Zdroj: | Proceedings of the National Academy of Sciences. 92:10526-10530 |
| ISSN: | 1091-6490 0027-8424 |
| Popis: | NMP-1 was initially identified as a nuclear matrix-associated DNA-binding factor that exhibits sequence-specific recognition for the site IV regulatory element of a histone H4 gene. This distal promoter domain is a nuclear matrix interaction site. In the present study, we show that NMP-1 is the multifunctional transcription factor YY1. Gel-shift and Western blot analyses demonstrate that NMP-1 is immunoreactive with YY1 antibody. Furthermore, purified YY1 protein specifically recognizes site IV and reconstitutes the NMP-1 complex. Western blot and gel-shift analyses indicate that YY1 is present within the nuclear matrix. In situ immunofluorescence studies show that a significant fraction of YY1 is localized in the nuclear matrix, principally but not exclusively associated with residual nucleoli. Our results confirm that NMP-1/YY1 is a ubiquitous protein that is present in both human cells and in rat osteosarcoma ROS 17/2.8 cells. The finding that NMP-1 is identical to YY1 suggests that this transcriptional regulator may mediate gene-matrix interactions. Our results are consistent with the concept that the nuclear matrix may functionally compartmentalize the eukaryotic nucleus to support regulation of gene expression. |
| Databáze: | OpenAIRE |
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