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Article: Mechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9
Title | Mechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9 |
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Authors | |
Keywords | DNA-Binding Proteins - genetics - metabolism Enhancer Elements (Genetics) High Mobility Group Proteins - genetics - metabolism Nuclear Proteins - genetics - metabolism Transcription Factors - genetics - metabolism |
Issue Date | 1999 |
Publisher | American Society for Microbiology. |
Citation | Molecular And Cellular Biology, 1999, v. 19 n. 1, p. 107-120 How to Cite? |
Abstract | SOX proteins bind similar DNA motifs through their high-mobility-group (HMG) domains, but their action is highly specific with respect to target genes and cell type. We investigated the mechanism of target selection by comparing SOX1/2/3, which activate δ-crystallin minimal enhancer DC5, with SOX9, which activates Col2a1 minimal enhancer COL2C2. These enhancers depend on both the SOX binding site and the binding site of a putative partner factor. The DC5 site was equally bound and bent by the HMG domains of SOX1/2 and SOX9. The activation domains of these SOX proteins mapped at the distal portions of the C-terminal domains were not cell specific and were independent of the partner factor. Chimeric proteins produced between SOX1 and SOX9 showed that to activate the DC5 enhancer, the C-terminal domain must be that of SOX1, although the HMG domains were replaceable. The SOX2-VP16 fusion protein, in which the activation domain of SOX2 was replaced by that of VP16, activated the DC5 enhancer still in a partner factor-dependent manner. The results argue that the proximal portion of the C-terminal domain of SOX1/2 specifically interacts with the partner factor, and this interaction determines the specificity of the SOX1/2 action. Essentially the same results were obtained in the converse experiments in which COL2C2 activation by SOX9 was analyzed, except that specificity of SOX9-partner factor interaction also involved the SOX9 HMG domain. The highly selective SOX-partner factor interactions presumably stabilize the DNA binding of the SOX proteins and provide the mechanism for regulatory target selection. |
Persistent Identifier | http://hdl.handle.net/10722/48974 |
ISSN | 2023 Impact Factor: 3.2 2023 SCImago Journal Rankings: 1.452 |
PubMed Central ID | |
ISI Accession Number ID | |
References |
DC Field | Value | Language |
---|---|---|
dc.contributor.author | Kamachi, Y | en_HK |
dc.contributor.author | Cheah, KSE | en_HK |
dc.contributor.author | Kondoh, H | en_HK |
dc.date.accessioned | 2008-06-12T06:31:09Z | - |
dc.date.available | 2008-06-12T06:31:09Z | - |
dc.date.issued | 1999 | en_HK |
dc.identifier.citation | Molecular And Cellular Biology, 1999, v. 19 n. 1, p. 107-120 | en_HK |
dc.identifier.issn | 0270-7306 | en_HK |
dc.identifier.uri | http://hdl.handle.net/10722/48974 | - |
dc.description.abstract | SOX proteins bind similar DNA motifs through their high-mobility-group (HMG) domains, but their action is highly specific with respect to target genes and cell type. We investigated the mechanism of target selection by comparing SOX1/2/3, which activate δ-crystallin minimal enhancer DC5, with SOX9, which activates Col2a1 minimal enhancer COL2C2. These enhancers depend on both the SOX binding site and the binding site of a putative partner factor. The DC5 site was equally bound and bent by the HMG domains of SOX1/2 and SOX9. The activation domains of these SOX proteins mapped at the distal portions of the C-terminal domains were not cell specific and were independent of the partner factor. Chimeric proteins produced between SOX1 and SOX9 showed that to activate the DC5 enhancer, the C-terminal domain must be that of SOX1, although the HMG domains were replaceable. The SOX2-VP16 fusion protein, in which the activation domain of SOX2 was replaced by that of VP16, activated the DC5 enhancer still in a partner factor-dependent manner. The results argue that the proximal portion of the C-terminal domain of SOX1/2 specifically interacts with the partner factor, and this interaction determines the specificity of the SOX1/2 action. Essentially the same results were obtained in the converse experiments in which COL2C2 activation by SOX9 was analyzed, except that specificity of SOX9-partner factor interaction also involved the SOX9 HMG domain. The highly selective SOX-partner factor interactions presumably stabilize the DNA binding of the SOX proteins and provide the mechanism for regulatory target selection. | en_HK |
dc.format.extent | 384 bytes | - |
dc.format.mimetype | text/html | - |
dc.language | eng | en_HK |
dc.publisher | American Society for Microbiology. | en_HK |
dc.relation.ispartof | Molecular and Cellular Biology | en_HK |
dc.rights | Molecular and Cellular Biology. Copyright © American Society for Microbiology. | en_HK |
dc.rights | Copyright © American Society for Microbiology, Molecular and Cellular Biology, 1999, v. 19 n. 1, p. 107-120 | en_HK |
dc.subject | DNA-Binding Proteins - genetics - metabolism | en_HK |
dc.subject | Enhancer Elements (Genetics) | en_HK |
dc.subject | High Mobility Group Proteins - genetics - metabolism | en_HK |
dc.subject | Nuclear Proteins - genetics - metabolism | en_HK |
dc.subject | Transcription Factors - genetics - metabolism | en_HK |
dc.title | Mechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9 | en_HK |
dc.type | Article | en_HK |
dc.identifier.openurl | http://library.hku.hk:4550/resserv?sid=HKU:IR&issn=0270-7306&volume=19&issue=1&spage=107&epage=120&date=1999&atitle=Mechanism+of+regulatory+target+selection+by+the+SOX+high-mobility-group+domain+proteins+as+revealed+by+comparison+of+SOX1/2/3+and+SOX9 | en_HK |
dc.identifier.email | Cheah, KSE:hrmbdkc@hku.hk | en_HK |
dc.identifier.authority | Cheah, KSE=rp00342 | en_HK |
dc.description.nature | published_or_final_version | en_HK |
dc.identifier.pmid | 9858536 | - |
dc.identifier.pmcid | PMC83870 | en_HK |
dc.identifier.scopus | eid_2-s2.0-0032927874 | en_HK |
dc.identifier.hkuros | 43288 | - |
dc.relation.references | http://www.scopus.com/mlt/select.url?eid=2-s2.0-0032927874&selection=ref&src=s&origin=recordpage | en_HK |
dc.identifier.volume | 19 | en_HK |
dc.identifier.issue | 1 | en_HK |
dc.identifier.spage | 107 | en_HK |
dc.identifier.epage | 120 | en_HK |
dc.identifier.isi | WOS:000077647100011 | - |
dc.publisher.place | United States | en_HK |
dc.identifier.scopusauthorid | Kamachi, Y=7004374984 | en_HK |
dc.identifier.scopusauthorid | Cheah, KSE=35387746200 | en_HK |
dc.identifier.scopusauthorid | Kondoh, H=7101792028 | en_HK |
dc.identifier.issnl | 0270-7306 | - |