Authors
Guo, BoOdgren, Paul R.
Van Wijnen, Andre J.
Last, Thomas J.
Nickerson, Jeffrey A.
Penman, Sheldon
Lian, Jane B.
Stein, Janet L.
Stein, Gary S.
Student Authors
Thomas J. LastUMass Chan Affiliations
Department of Cell BiologyDocument Type
Journal ArticlePublication Date
1995-11-07Keywords
Animals; Antibody Specificity; Base Sequence; Binding Sites; Blotting, Western; Cell Compartmentation; Cell Nucleolus; Cell Nucleus; Cross Reactions; DNA; DNA-Binding Proteins; purification; Erythroid-Specific DNA-Binding Factors; Hela Cells; Humans; Molecular Sequence Data; Nuclear Matrix; Oligodeoxyribonucleotides; Protein Binding; Rats; Recombinant Proteins; Transcription Factors; purification; YY1 Transcription FactorCell Biology
Life Sciences
Medicine and Health Sciences
Metadata
Show full item recordAbstract
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.Source
Proc Natl Acad Sci U S A. 1995 Nov 7;92(23):10526-30.
DOI
10.1073/pnas.92.23.10526Permanent Link to this Item
http://hdl.handle.net/20.500.14038/33795PubMed ID
7479833Related Resources
ae974a485f413a2113503eed53cd6c53
10.1073/pnas.92.23.10526