Critical Reviews™ in Eukaryotic Gene Expression

ISSN for PRINT: 1045-4403

For Online Access

Best Paper Award Selection - Editorial Board Site

2001, Volume11

Issue 4

73 pages

Issue price - $169.00

Joseph P. Bidwell, Ph.D.
Department of Anatomy and Cell Biology; Department of Periodontics, Indiana University, School of Dentistry, Indianapolis, IN 46202

Kitti Torrungruang
Department of Periodontics, Indiana University School of Dentistry, Indianapolis, IN 46202

Marta Alvarez
Department of Anatomy and Cell Biology, Indiana University School of Dentistry, Indianapolis, IN 46202

Simon J. Rhodes
Department of Biology, Indiana University—Purdue University Indianapolis, Indianapolis, IN 46202

Rita Shah
Department of Periodontics, Indiana University School of Dentistry, Indianapolis, IN 46202

Daniel R. Jones
Department of Anatomy and Cell Biology, Indiana University School of Dentistry, Indianapolis, IN 46202

Kanokwan Charoonpatrapong
Department of Anatomy and Cell Biology, Indiana University School of Dentistry, Indianapolis, IN 46202

Janet M. Hock
Department of Anatomy and Cell Biology; Department of Periodontics, Indiana University School of Dentistry, Indianapolis, IN 46202

Andrew J. Watt
University of Michigan Medical School, Ann Arbor, MI 48109

The functional role of the osteoblast nuclear matrix has been a matter of supposition. Its presumed func tion as an architectural agent of transcription derives primarily from the low solubility of nuclear matrix proteins and their typical localization into discrete subnuclear domains. In addressing how the nuclear matrix regulates skeletal genes, the authors compare Nmp4, Cbfa1, and YY1 for the purpose of profiling osteoblast nuclear matrix trans cription factors. All three proteins contribute to the trans cription of ECM gene s and partition int o the osteoblast nuclear matrix via a nuclear matrix targeting domain. The authors propose that osteoblast nuclear matrix transcription factors involved in ECM regulation generally have the capacity to alter DNA geometry and reciprocally respond to DNA as an allosteric ligand. This may allow these proteins to adapt to the local nuclear architecture and generate the pattern of regulation specified by that architecture via unmasking of the appropriate transactivation domains. Osteoblast nuclear matrix transcription factors may also act as transcriptional adaptor molecules by supporting the formation of higher order protein complexes along target gene promoters. The genes encoding all three proteins considered here have trinucleotide repeat domains, although the significance of this is unclear. There is no canonical nuclear matrix binding motif, but finger-like structures may be suited for anchoring proteins to discrete subnuclear domains. Finally, the ability to leave the osteoblast nuclear matrix may be as important to the function of some nuclear matrix transcription factors as their association with this subcompartment.

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