Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells
TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other transcription factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus...
Gespeichert in:
Veröffentlicht in: | Applied biochemistry and biotechnology 2016-06, Vol.179 (4), p.650-658 |
---|---|
Hauptverfasser: | , , |
Format: | Artikel |
Sprache: | eng |
Schlagworte: | |
Online-Zugang: | Volltext |
Tags: |
Tag hinzufügen
Keine Tags, Fügen Sie den ersten Tag hinzu!
|
container_end_page | 658 |
---|---|
container_issue | 4 |
container_start_page | 650 |
container_title | Applied biochemistry and biotechnology |
container_volume | 179 |
creator | Kim, Chang Min Jang, Tae-ho Park, Hyun Ho |
description | TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other transcription factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus and the SAM-like domain at the C-terminus. In this study, we found that TFCP2L1 is hexamerized in solution via the C-terminal SAM-like domain. We also found that homo-oligomerization of SAM-like domain is dependent on the concentration of the proteins. Finally, we found that TFCP2L1 binds directly to DNA via the N-terminal CP2-like domain. |
doi_str_mv | 10.1007/s12010-016-2021-z |
format | Article |
fullrecord | <record><control><sourceid>proquest_cross</sourceid><recordid>TN_cdi_proquest_miscellaneous_1808736792</recordid><sourceformat>XML</sourceformat><sourcesystem>PC</sourcesystem><sourcerecordid>4099785161</sourcerecordid><originalsourceid>FETCH-LOGICAL-c442t-3bc63a0fb7730165d285c334ee1e3dd7722dade489deb80253cbcb35b695c1e83</originalsourceid><addsrcrecordid>eNqFkVFLHDEUhUNR6mr7A_oiAV_60GhusjOZPC6rawurFbTPIZO5K2NnJmsyU7r-erOMFSuIEBJIvntyzz2EfAF-DJyrkwiCA2cccia4APbwgUwgyzTjQsMOmXChJBOi0HtkP8Y7zkEUmfpI9kSueQ5QTMjfxdC5vvadbegsbZtYR-pXdH4l2LL-jfTUt7buqO0qej27-O8urZtFApfwjV76P9jQq2YI9dr32LkNXVjX-7AVO2vLsPFd7eh1jy2dY9PET2R3ZZuIn5_OA_JrcXYz_86WP89_zGdL5qZT0TNZulxaviqVkslnViUHTsopIqCsKqWEqGyF00JXWBZcZNKVrpRZmevMARbygHwdddfB3w8Ye9PW0aUObId-iAYKXiiZKy3eR5XWabq5hoQevULv_BDS_EZKpi5lnigYKRd8jAFXZh3q1oaNAW62CZoxQZOcmW2C5iHVHD4pD2WL1XPFv8gSIEYgpqfuFsOLr99UfQRHS6P6</addsrcrecordid><sourcetype>Aggregation Database</sourcetype><iscdi>true</iscdi><recordtype>article</recordtype><pqid>1799328536</pqid></control><display><type>article</type><title>Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells</title><source>MEDLINE</source><source>Springer Nature - Complete Springer Journals</source><creator>Kim, Chang Min ; Jang, Tae-ho ; Park, Hyun Ho</creator><creatorcontrib>Kim, Chang Min ; Jang, Tae-ho ; Park, Hyun Ho</creatorcontrib><description>TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other transcription factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus and the SAM-like domain at the C-terminus. In this study, we found that TFCP2L1 is hexamerized in solution via the C-terminal SAM-like domain. We also found that homo-oligomerization of SAM-like domain is dependent on the concentration of the proteins. Finally, we found that TFCP2L1 binds directly to DNA via the N-terminal CP2-like domain.</description><identifier>ISSN: 0273-2289</identifier><identifier>EISSN: 1559-0291</identifier><identifier>DOI: 10.1007/s12010-016-2021-z</identifier><identifier>PMID: 26906118</identifier><language>eng</language><publisher>New York: Springer US</publisher><subject>Animals ; Biochemistry ; Biotechnology ; Cell Differentiation - genetics ; Chemistry ; Chemistry and Materials Science ; DNA-Binding Proteins - chemistry ; DNA-Binding Proteins - genetics ; DNA-Binding Proteins - metabolism ; Embryonic Stem Cells - chemistry ; Embryonic Stem Cells - metabolism ; Embryos ; Mice ; Nanog Homeobox Protein - genetics ; Nanog Homeobox Protein - metabolism ; Octamer Transcription Factor-3 - genetics ; Octamer Transcription Factor-3 - metabolism ; Protein Domains - genetics ; Protein Multimerization ; Proteins ; Repressor Proteins - chemistry ; Repressor Proteins - genetics ; Repressor Proteins - metabolism ; SOXB1 Transcription Factors - genetics ; SOXB1 Transcription Factors - metabolism ; Stem cells ; Transcription factors</subject><ispartof>Applied biochemistry and biotechnology, 2016-06, Vol.179 (4), p.650-658</ispartof><rights>Springer Science+Business Media New York 2016</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c442t-3bc63a0fb7730165d285c334ee1e3dd7722dade489deb80253cbcb35b695c1e83</citedby><cites>FETCH-LOGICAL-c442t-3bc63a0fb7730165d285c334ee1e3dd7722dade489deb80253cbcb35b695c1e83</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://link.springer.com/content/pdf/10.1007/s12010-016-2021-z$$EPDF$$P50$$Gspringer$$H</linktopdf><linktohtml>$$Uhttps://link.springer.com/10.1007/s12010-016-2021-z$$EHTML$$P50$$Gspringer$$H</linktohtml><link.rule.ids>314,777,781,27905,27906,41469,42538,51300</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/26906118$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Kim, Chang Min</creatorcontrib><creatorcontrib>Jang, Tae-ho</creatorcontrib><creatorcontrib>Park, Hyun Ho</creatorcontrib><title>Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells</title><title>Applied biochemistry and biotechnology</title><addtitle>Appl Biochem Biotechnol</addtitle><addtitle>Appl Biochem Biotechnol</addtitle><description>TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other transcription factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus and the SAM-like domain at the C-terminus. In this study, we found that TFCP2L1 is hexamerized in solution via the C-terminal SAM-like domain. We also found that homo-oligomerization of SAM-like domain is dependent on the concentration of the proteins. Finally, we found that TFCP2L1 binds directly to DNA via the N-terminal CP2-like domain.</description><subject>Animals</subject><subject>Biochemistry</subject><subject>Biotechnology</subject><subject>Cell Differentiation - genetics</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>DNA-Binding Proteins - chemistry</subject><subject>DNA-Binding Proteins - genetics</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Embryonic Stem Cells - chemistry</subject><subject>Embryonic Stem Cells - metabolism</subject><subject>Embryos</subject><subject>Mice</subject><subject>Nanog Homeobox Protein - genetics</subject><subject>Nanog Homeobox Protein - metabolism</subject><subject>Octamer Transcription Factor-3 - genetics</subject><subject>Octamer Transcription Factor-3 - metabolism</subject><subject>Protein Domains - genetics</subject><subject>Protein Multimerization</subject><subject>Proteins</subject><subject>Repressor Proteins - chemistry</subject><subject>Repressor Proteins - genetics</subject><subject>Repressor Proteins - metabolism</subject><subject>SOXB1 Transcription Factors - genetics</subject><subject>SOXB1 Transcription Factors - metabolism</subject><subject>Stem cells</subject><subject>Transcription factors</subject><issn>0273-2289</issn><issn>1559-0291</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><sourceid>ABUWG</sourceid><sourceid>AFKRA</sourceid><sourceid>AZQEC</sourceid><sourceid>BENPR</sourceid><sourceid>CCPQU</sourceid><sourceid>DWQXO</sourceid><sourceid>GNUQQ</sourceid><recordid>eNqFkVFLHDEUhUNR6mr7A_oiAV_60GhusjOZPC6rawurFbTPIZO5K2NnJmsyU7r-erOMFSuIEBJIvntyzz2EfAF-DJyrkwiCA2cccia4APbwgUwgyzTjQsMOmXChJBOi0HtkP8Y7zkEUmfpI9kSueQ5QTMjfxdC5vvadbegsbZtYR-pXdH4l2LL-jfTUt7buqO0qej27-O8urZtFApfwjV76P9jQq2YI9dr32LkNXVjX-7AVO2vLsPFd7eh1jy2dY9PET2R3ZZuIn5_OA_JrcXYz_86WP89_zGdL5qZT0TNZulxaviqVkslnViUHTsopIqCsKqWEqGyF00JXWBZcZNKVrpRZmevMARbygHwdddfB3w8Ye9PW0aUObId-iAYKXiiZKy3eR5XWabq5hoQevULv_BDS_EZKpi5lnigYKRd8jAFXZh3q1oaNAW62CZoxQZOcmW2C5iHVHD4pD2WL1XPFv8gSIEYgpqfuFsOLr99UfQRHS6P6</recordid><startdate>20160601</startdate><enddate>20160601</enddate><creator>Kim, Chang Min</creator><creator>Jang, Tae-ho</creator><creator>Park, Hyun Ho</creator><general>Springer US</general><general>Springer Nature B.V</general><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>3V.</scope><scope>7ST</scope><scope>7T7</scope><scope>7TM</scope><scope>7X7</scope><scope>7XB</scope><scope>88A</scope><scope>88E</scope><scope>88I</scope><scope>8AO</scope><scope>8FD</scope><scope>8FE</scope><scope>8FH</scope><scope>8FI</scope><scope>8FJ</scope><scope>8FK</scope><scope>ABUWG</scope><scope>AEUYN</scope><scope>AFKRA</scope><scope>AZQEC</scope><scope>BBNVY</scope><scope>BENPR</scope><scope>BHPHI</scope><scope>C1K</scope><scope>CCPQU</scope><scope>DWQXO</scope><scope>FR3</scope><scope>FYUFA</scope><scope>GHDGH</scope><scope>GNUQQ</scope><scope>HCIFZ</scope><scope>K9.</scope><scope>LK8</scope><scope>M0S</scope><scope>M1P</scope><scope>M2P</scope><scope>M7P</scope><scope>P64</scope><scope>PQEST</scope><scope>PQQKQ</scope><scope>PQUKI</scope><scope>Q9U</scope><scope>RC3</scope><scope>SOI</scope><scope>7X8</scope><scope>7QO</scope></search><sort><creationdate>20160601</creationdate><title>Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells</title><author>Kim, Chang Min ; Jang, Tae-ho ; Park, Hyun Ho</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c442t-3bc63a0fb7730165d285c334ee1e3dd7722dade489deb80253cbcb35b695c1e83</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Animals</topic><topic>Biochemistry</topic><topic>Biotechnology</topic><topic>Cell Differentiation - genetics</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - genetics</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Embryonic Stem Cells - chemistry</topic><topic>Embryonic Stem Cells - metabolism</topic><topic>Embryos</topic><topic>Mice</topic><topic>Nanog Homeobox Protein - genetics</topic><topic>Nanog Homeobox Protein - metabolism</topic><topic>Octamer Transcription Factor-3 - genetics</topic><topic>Octamer Transcription Factor-3 - metabolism</topic><topic>Protein Domains - genetics</topic><topic>Protein Multimerization</topic><topic>Proteins</topic><topic>Repressor Proteins - chemistry</topic><topic>Repressor Proteins - genetics</topic><topic>Repressor Proteins - metabolism</topic><topic>SOXB1 Transcription Factors - genetics</topic><topic>SOXB1 Transcription Factors - metabolism</topic><topic>Stem cells</topic><topic>Transcription factors</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Kim, Chang Min</creatorcontrib><creatorcontrib>Jang, Tae-ho</creatorcontrib><creatorcontrib>Park, Hyun Ho</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>ProQuest Central (Corporate)</collection><collection>Environment Abstracts</collection><collection>Industrial and Applied Microbiology Abstracts (Microbiology A)</collection><collection>Nucleic Acids Abstracts</collection><collection>Health & Medical Collection</collection><collection>ProQuest Central (purchase pre-March 2016)</collection><collection>Biology Database (Alumni Edition)</collection><collection>Medical Database (Alumni Edition)</collection><collection>Science Database (Alumni Edition)</collection><collection>ProQuest Pharma Collection</collection><collection>Technology Research Database</collection><collection>ProQuest SciTech Collection</collection><collection>ProQuest Natural Science Collection</collection><collection>Hospital Premium Collection</collection><collection>Hospital Premium Collection (Alumni Edition)</collection><collection>ProQuest Central (Alumni) (purchase pre-March 2016)</collection><collection>ProQuest Central (Alumni Edition)</collection><collection>ProQuest One Sustainability</collection><collection>ProQuest Central UK/Ireland</collection><collection>ProQuest Central Essentials</collection><collection>Biological Science Collection</collection><collection>ProQuest Central</collection><collection>Natural Science Collection</collection><collection>Environmental Sciences and Pollution Management</collection><collection>ProQuest One Community College</collection><collection>ProQuest Central Korea</collection><collection>Engineering Research Database</collection><collection>Health Research Premium Collection</collection><collection>Health Research Premium Collection (Alumni)</collection><collection>ProQuest Central Student</collection><collection>SciTech Premium Collection</collection><collection>ProQuest Health & Medical Complete (Alumni)</collection><collection>ProQuest Biological Science Collection</collection><collection>Health & Medical Collection (Alumni Edition)</collection><collection>Medical Database</collection><collection>Science Database</collection><collection>Biological Science Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><collection>ProQuest One Academic Eastern Edition (DO NOT USE)</collection><collection>ProQuest One Academic</collection><collection>ProQuest One Academic UKI Edition</collection><collection>ProQuest Central Basic</collection><collection>Genetics Abstracts</collection><collection>Environment Abstracts</collection><collection>MEDLINE - Academic</collection><collection>Biotechnology Research Abstracts</collection><jtitle>Applied biochemistry and biotechnology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Kim, Chang Min</au><au>Jang, Tae-ho</au><au>Park, Hyun Ho</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells</atitle><jtitle>Applied biochemistry and biotechnology</jtitle><stitle>Appl Biochem Biotechnol</stitle><addtitle>Appl Biochem Biotechnol</addtitle><date>2016-06-01</date><risdate>2016</risdate><volume>179</volume><issue>4</issue><spage>650</spage><epage>658</epage><pages>650-658</pages><issn>0273-2289</issn><eissn>1559-0291</eissn><abstract>TFCP2L1 is a transcription factor that facilitates establishment and maintenance of pluripotency in embryonic stem cells by forming a complex transcriptional network with other transcription factors (OCT4, SOX2, and NANOG). TFCP2L1 contains two distinct domains, the CP2-like domain at the N-terminus and the SAM-like domain at the C-terminus. In this study, we found that TFCP2L1 is hexamerized in solution via the C-terminal SAM-like domain. We also found that homo-oligomerization of SAM-like domain is dependent on the concentration of the proteins. Finally, we found that TFCP2L1 binds directly to DNA via the N-terminal CP2-like domain.</abstract><cop>New York</cop><pub>Springer US</pub><pmid>26906118</pmid><doi>10.1007/s12010-016-2021-z</doi><tpages>9</tpages></addata></record> |
fulltext | fulltext |
identifier | ISSN: 0273-2289 |
ispartof | Applied biochemistry and biotechnology, 2016-06, Vol.179 (4), p.650-658 |
issn | 0273-2289 1559-0291 |
language | eng |
recordid | cdi_proquest_miscellaneous_1808736792 |
source | MEDLINE; Springer Nature - Complete Springer Journals |
subjects | Animals Biochemistry Biotechnology Cell Differentiation - genetics Chemistry Chemistry and Materials Science DNA-Binding Proteins - chemistry DNA-Binding Proteins - genetics DNA-Binding Proteins - metabolism Embryonic Stem Cells - chemistry Embryonic Stem Cells - metabolism Embryos Mice Nanog Homeobox Protein - genetics Nanog Homeobox Protein - metabolism Octamer Transcription Factor-3 - genetics Octamer Transcription Factor-3 - metabolism Protein Domains - genetics Protein Multimerization Proteins Repressor Proteins - chemistry Repressor Proteins - genetics Repressor Proteins - metabolism SOXB1 Transcription Factors - genetics SOXB1 Transcription Factors - metabolism Stem cells Transcription factors |
title | Functional Analysis of CP2-Like Domain and SAM-Like Domain in TFCP2L1, Novel Pluripotency Factor of Embryonic Stem Cells |
url | https://sfx.bib-bvb.de/sfx_tum?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-20T13%3A13%3A50IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-proquest_cross&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Functional%20Analysis%20of%20CP2-Like%20Domain%20and%20SAM-Like%20Domain%20in%20TFCP2L1,%20Novel%20Pluripotency%20Factor%20of%20Embryonic%20Stem%20Cells&rft.jtitle=Applied%20biochemistry%20and%20biotechnology&rft.au=Kim,%20Chang%20Min&rft.date=2016-06-01&rft.volume=179&rft.issue=4&rft.spage=650&rft.epage=658&rft.pages=650-658&rft.issn=0273-2289&rft.eissn=1559-0291&rft_id=info:doi/10.1007/s12010-016-2021-z&rft_dat=%3Cproquest_cross%3E4099785161%3C/proquest_cross%3E%3Curl%3E%3C/url%3E&disable_directlink=true&sfx.directlink=off&sfx.report_link=0&rft_id=info:oai/&rft_pqid=1799328536&rft_id=info:pmid/26906118&rfr_iscdi=true |