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

Bo Guo, Paul R. Odgren, André J. Van Wunen, Thomas J. Last, Jeffrey Nickerson, Sheldon Penman, Jane B. Lian, Janet L. Stein, Gary S. Stein

Research output: Contribution to journalArticlepeer-review

159 Scopus citations

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 thai 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.

Original languageEnglish (US)
Pages (from-to)10526-10530
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume92
Issue number23
DOIs
StatePublished - Nov 7 1995

Keywords

  • gene expression
  • histone H4
  • nuclear structure
  • nucleolus
  • osteoblast

ASJC Scopus subject areas

  • General

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