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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

TitleMechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9
Authors
KeywordsDNA-Binding Proteins - genetics - metabolism
Enhancer Elements (Genetics)
High Mobility Group Proteins - genetics - metabolism
Nuclear Proteins - genetics - metabolism
Transcription Factors - genetics - metabolism
Issue Date1999
PublisherAmerican Society for Microbiology.
Citation
Molecular And Cellular Biology, 1999, v. 19 n. 1, p. 107-120 How to Cite?
AbstractSOX 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 Identifierhttp://hdl.handle.net/10722/48974
ISSN
2015 Impact Factor: 4.427
2015 SCImago Journal Rankings: 3.806
PubMed Central ID
ISI Accession Number ID
References

 

DC FieldValueLanguage
dc.contributor.authorKamachi, Yen_HK
dc.contributor.authorCheah, KSEen_HK
dc.contributor.authorKondoh, Hen_HK
dc.date.accessioned2008-06-12T06:31:09Z-
dc.date.available2008-06-12T06:31:09Z-
dc.date.issued1999en_HK
dc.identifier.citationMolecular And Cellular Biology, 1999, v. 19 n. 1, p. 107-120en_HK
dc.identifier.issn0270-7306en_HK
dc.identifier.urihttp://hdl.handle.net/10722/48974-
dc.description.abstractSOX 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.extent384 bytes-
dc.format.mimetypetext/html-
dc.languageengen_HK
dc.publisherAmerican Society for Microbiology.en_HK
dc.relation.ispartofMolecular and Cellular Biologyen_HK
dc.rightsMolecular and Cellular Biology. Copyright © American Society for Microbiology.en_HK
dc.rightsCreative Commons: Attribution 3.0 Hong Kong License-
dc.rightsCopyright © American Society for Microbiology, Molecular and Cellular Biology, 1999, v. 19 n. 1, p. 107-120en_HK
dc.subjectDNA-Binding Proteins - genetics - metabolismen_HK
dc.subjectEnhancer Elements (Genetics)en_HK
dc.subjectHigh Mobility Group Proteins - genetics - metabolismen_HK
dc.subjectNuclear Proteins - genetics - metabolismen_HK
dc.subjectTranscription Factors - genetics - metabolismen_HK
dc.titleMechanism of regulatory target selection by the SOX high-mobility-group domain proteins as revealed by comparison of SOX1/2/3 and SOX9en_HK
dc.typeArticleen_HK
dc.identifier.openurlhttp://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+SOX9en_HK
dc.identifier.emailCheah, KSE:hrmbdkc@hku.hken_HK
dc.identifier.authorityCheah, KSE=rp00342en_HK
dc.description.naturepublished_or_final_versionen_HK
dc.identifier.pmid9858536-
dc.identifier.pmcidPMC83870en_HK
dc.identifier.scopuseid_2-s2.0-0032927874en_HK
dc.identifier.hkuros43288-
dc.relation.referenceshttp://www.scopus.com/mlt/select.url?eid=2-s2.0-0032927874&selection=ref&src=s&origin=recordpageen_HK
dc.identifier.volume19en_HK
dc.identifier.issue1en_HK
dc.identifier.spage107en_HK
dc.identifier.epage120en_HK
dc.identifier.isiWOS:000077647100011-
dc.publisher.placeUnited Statesen_HK
dc.identifier.scopusauthoridKamachi, Y=7004374984en_HK
dc.identifier.scopusauthoridCheah, KSE=35387746200en_HK
dc.identifier.scopusauthoridKondoh, H=7101792028en_HK

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