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dc.contributor.authorMerriman, Harold L.
dc.contributor.authorVan Wijnen, Andre J.
dc.contributor.authorHiebert, Scott W.
dc.contributor.authorBidwell, Joseph P.
dc.contributor.authorFey, Edward G.
dc.contributor.authorLian, Jane B.
dc.contributor.authorStein, Janet L.
dc.contributor.authorStein, Gary S.
dc.date2022-08-11T08:09:02.000
dc.date.accessioned2022-08-23T16:15:54Z
dc.date.available2022-08-23T16:15:54Z
dc.date.issued1995-10-10
dc.date.submitted2008-11-21
dc.identifier.citation<p>Biochemistry. 1995 Oct 10;34(40):13125-32.</p>
dc.identifier.issn0006-2960 (Print)
dc.identifier.doi10.1021/bi00040a025
dc.identifier.pmid7548073
dc.identifier.urihttp://hdl.handle.net/20.500.14038/34204
dc.description.abstractThe 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.
dc.language.isoen_US
dc.relation<p><a href="http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=7548073&dopt=Abstract">Link to article in PubMed</a></p>
dc.relation.urlhttps://doi.org/10.1021/bi00040a025
dc.subjectAnimals; Base Sequence; Consensus Sequence; DNA-Binding Proteins; Gene Expression Regulation; Molecular Sequence Data; Nuclear Matrix; Nuclear Proteins; Oligodeoxyribonucleotides; Osteocalcin; Promoter Regions (Genetics); Rats; Transcription Factors; Tumor Cells, Cultured
dc.subjectLife Sciences
dc.subjectMedicine and Health Sciences
dc.titleThe 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
dc.typeJournal Article
dc.source.journaltitleBiochemistry
dc.source.volume34
dc.source.issue40
dc.identifier.legacycoverpagehttps://escholarship.umassmed.edu/gsbs_sp/860
dc.identifier.contextkey670706
html.description.abstract<p>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.</p>
dc.identifier.submissionpathgsbs_sp/860
dc.contributor.departmentDepartment of Cell Biology
dc.contributor.departmentGraduate School of Biomedical Sciences
dc.source.pages13125-32


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