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The tissue-specific nuclear matrix protein, NMP-2, is a member of the AML/CBF/PEBP2/runt domain transcription factor family: interactions with the osteocalcin gene promoter
Authors
Merriman, Harold L.Van Wijnen, Andre J.
Hiebert, Scott W.
Bidwell, Joseph P.
Fey, Edward G.
Lian, Jane B.
Stein, Janet L.
Stein, Gary S.
UMass Chan Affiliations
Department of Cell BiologyMorningside Graduate School of Biomedical Sciences
Document Type
Journal ArticlePublication Date
1995-10-10
Metadata
Show full item recordAbstract
The nuclear matrix protein, NMP-2, was originally identified as an osteoblast-specific DNA-binding complex localized exclusively to the nuclear matrix. NMP-2 was shown to recognize two binding sites, site A (nt-605 to -599) and site B (nt -441 to -435), in the rat bone-specific osteocalcin gene promoter. This study shows that the NMP-2 binding sites A and B as well as a third NMP-2 binding site (nt -135 to -130) constitute a consensus sequence, ATGCTGGT, and represent an AML-1 recognition motif. AML-1 is a member of the AML transcription factor family which is associated with acute myelogenous leukemia and binds to the sequence TGCTGGT via its DNA-binding runt domain. Electrophoretic mobility shift assays reveal that a component of NMP-2 is a member of the AML/PEBP2/runt domain transcription factor family based on cross-competition with AML-1 consensus oligonucleotide. Limited immunoreactivity of NMP-2 with a polyclonal N-terminal AML-1 antibody and inability of the AML-1 partner protein CBF-beta to form complexes with NMP-2 indicate that NMP-2 is not identical to AML-1 but represents a variant AML/PEBP2/runt domain protein. Western and Northern blots reveal the presence of multiple AML-related proteins and AML-1 transcripts in several osseous cell lines. Furthermore, our results indicate that AML family members may selectively partition between nuclear matrix and nonmatrix compartments. Because proteins that contain a runt domain are implicated in tissue-specific transcriptional regulation, our results support the concept that the nuclear matrix mediates osteoblast-specific expression of the osteocalcin gene.Source
Biochemistry. 1995 Oct 10;34(40):13125-32.
DOI
10.1021/bi00040a025Permanent Link to this Item
http://hdl.handle.net/20.500.14038/34204PubMed ID
7548073Related Resources
ae974a485f413a2113503eed53cd6c53
10.1021/bi00040a025