NDLI: The nuclear matrix protein NMP-1 is the transcription factor YY1.

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The nuclear matrix protein NMP-1 is the transcription factor YY1.

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The nuclear matrix protein NMP-1 is the transcription factor YY1.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Last, T. J. Nickerson, J. Guo, B. Lian, J. B. Penman, S. Van Wijnen, A. J. Odgren, P. R. Stein, G. S. Stein, J. L.
Description	Author Affiliation: Guo B ( Department of Cell Biology, University of Masachusetts Medical Center, Worcester 01655, USA.);
Abstract	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.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	23
Volume Number	92
Language	English
Publisher	National Academy of Sciences
Publisher Date	1995-12-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Cell Nucleus Chemistry DNA-Binding Proteins Isolation & Purification Transcription Factors Animals Antibody Specificity Binding Sites Blotting, Western Cell Compartmentation Cell Nucleolus Ultrastructure Cross Reactions DNA Metabolism Genetics Immunology Erythroid-Specific DNA-Binding Factors HeLa Cells Molecular Sequence Data Nuclear Matrix Oligodeoxyribonucleotides Protein Binding Recombinant Proteins YY1 Transcription Factor Research Support, U.S. Gov't, P.H.S. Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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