Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor
The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous...
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| Veröffentlicht in: | Journal of cellular biochemistry 2007-06, Vol.101 (3), p.785-789 |
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| container_title | Journal of cellular biochemistry |
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| creator | Bruna, Carola Arriagada, Gloria Lian, Jane B Stein, Gary S Bunster, Marta Martinez-Oyanedel, Jose Montecino, Martin |
| description | The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR-Runx2 interaction are contained within the 230-361 domain of Runx2. In this work, we confirmed by GST-pull down that Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(209-361)) protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 A and a complete data set to a 3.3 A resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P4 and unit-cell parameters of a = b = 90.8, and c = 57.2 A. The presence of a monomer of the recombinant GST-Runx2(I(209-361)) in the asymmetric unit gives a V(M) of 2.7 A(3) Da(-1) and a solvent content of 54.8%. |
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In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR-Runx2 interaction are contained within the 230-361 domain of Runx2. In this work, we confirmed by GST-pull down that Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(209-361)) protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 A and a complete data set to a 3.3 A resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P4 and unit-cell parameters of a = b = 90.8, and c = 57.2 A. 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In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR-Runx2 interaction are contained within the 230-361 domain of Runx2. In this work, we confirmed by GST-pull down that Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(209-361)) protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 A and a complete data set to a 3.3 A resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P4 and unit-cell parameters of a = b = 90.8, and c = 57.2 A. The presence of a monomer of the recombinant GST-Runx2(I(209-361)) in the asymmetric unit gives a V(M) of 2.7 A(3) Da(-1) and a solvent content of 54.8%.</description><subject>Absorptiometry, Photon - methods</subject><subject>Animals</subject><subject>Core Binding Factor Alpha 1 Subunit - chemistry</subject><subject>Core Binding Factor Alpha 1 Subunit - genetics</subject><subject>Core Binding Factor Alpha 1 Subunit - metabolism</subject><subject>Crystallization - methods</subject><subject>Mice</subject><subject>Protein Binding</subject><subject>Protein Structure, Tertiary</subject><subject>Receptors, Calcitriol - genetics</subject><subject>Receptors, Calcitriol - metabolism</subject><issn>0730-2312</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2007</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo1kNtKxDAQhnOhuOvqK0iuvLKQQ5s0l7IeYUGQvfCuzKYpjaQHk1S3PosPa1hXGBhm5vv_gf8ELYnkJGOcsgU6D-GdEKIUZ2doQSVjQkq1RD9rP4cIztlviHboMfQ1Hr1xtrM9-Bm_ZR7mtAU3Bxvw0GDA9dCB7XGq2Br8OvV7hqOHPmhvx4NLAzoOPp0hJiwan-aAv2xsDxIKbmzhhhW4tu1c-2E_408bIf3Edxx7o82Y9BfotAEXzOWxr9D24X67fso2L4_P69tNNha5ynROhNRUFJTrpmBcUVlTCbzkfKcKUvJGiJLSkoi6EKAbrpmmShQq15xI2fAVuv6zHf3wMZkQq84GbZyD3gxTqCTJc6JymsCrIzjtOlNXo7ddyqj6j5P_AndZcaI</recordid><startdate>20070601</startdate><enddate>20070601</enddate><creator>Bruna, Carola</creator><creator>Arriagada, Gloria</creator><creator>Lian, Jane B</creator><creator>Stein, Gary S</creator><creator>Bunster, Marta</creator><creator>Martinez-Oyanedel, Jose</creator><creator>Montecino, Martin</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>7X8</scope></search><sort><creationdate>20070601</creationdate><title>Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor</title><author>Bruna, Carola ; Arriagada, Gloria ; Lian, Jane B ; Stein, Gary S ; Bunster, Marta ; Martinez-Oyanedel, Jose ; Montecino, Martin</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-p549-c4067c16513cf523917d17a3833b95083f66811806d56acf3c2c196594c3077f3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2007</creationdate><topic>Absorptiometry, Photon - methods</topic><topic>Animals</topic><topic>Core Binding Factor Alpha 1 Subunit - chemistry</topic><topic>Core Binding Factor Alpha 1 Subunit - genetics</topic><topic>Core Binding Factor Alpha 1 Subunit - metabolism</topic><topic>Crystallization - methods</topic><topic>Mice</topic><topic>Protein Binding</topic><topic>Protein Structure, Tertiary</topic><topic>Receptors, Calcitriol - genetics</topic><topic>Receptors, Calcitriol - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bruna, Carola</creatorcontrib><creatorcontrib>Arriagada, Gloria</creatorcontrib><creatorcontrib>Lian, Jane B</creatorcontrib><creatorcontrib>Stein, Gary S</creatorcontrib><creatorcontrib>Bunster, Marta</creatorcontrib><creatorcontrib>Martinez-Oyanedel, Jose</creatorcontrib><creatorcontrib>Montecino, Martin</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>MEDLINE - Academic</collection><jtitle>Journal of cellular biochemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bruna, Carola</au><au>Arriagada, Gloria</au><au>Lian, Jane B</au><au>Stein, Gary S</au><au>Bunster, Marta</au><au>Martinez-Oyanedel, Jose</au><au>Montecino, Martin</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor</atitle><jtitle>Journal of cellular biochemistry</jtitle><addtitle>J Cell Biochem</addtitle><date>2007-06-01</date><risdate>2007</risdate><volume>101</volume><issue>3</issue><spage>785</spage><epage>789</epage><pages>785-789</pages><issn>0730-2312</issn><abstract>The Runx2 transcription factor is a key regulator of osteoblast differentiation. In response to 1alpha,25 dihydroxy vitamin D3, Runx2 may interact with the 1alpha,25 dihydroxy vitamin D3 receptor (VDR) in the promoter of target genes, producing a synergic activation of their transcription. Previous studies have suggested that the motifs responsible for the VDR-Runx2 interaction are contained within the 230-361 domain of Runx2. In this work, we confirmed by GST-pull down that Runx2(I(209-361)) is sufficient to interact with the VDR. To obtain structural information, GST-Runx2(I(209-361)) protein was overexpressed in Escherichia coli, purified and crystallized using the hanging-drop vapor-diffusion method and polyethyleneglycol as a precipitant. The crystals were found to diffract to a maximum resolution of 2.7 A and a complete data set to a 3.3 A resolution was collected and analyzed. The crystals belong to the tetragonal system, with a space group P4 and unit-cell parameters of a = b = 90.8, and c = 57.2 A. The presence of a monomer of the recombinant GST-Runx2(I(209-361)) in the asymmetric unit gives a V(M) of 2.7 A(3) Da(-1) and a solvent content of 54.8%.</abstract><cop>United States</cop><pmid>17226779</pmid><tpages>5</tpages></addata></record> |
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| ispartof | Journal of cellular biochemistry, 2007-06, Vol.101 (3), p.785-789 |
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| subjects | Absorptiometry, Photon - methods Animals Core Binding Factor Alpha 1 Subunit - chemistry Core Binding Factor Alpha 1 Subunit - genetics Core Binding Factor Alpha 1 Subunit - metabolism Crystallization - methods Mice Protein Binding Protein Structure, Tertiary Receptors, Calcitriol - genetics Receptors, Calcitriol - metabolism |
| title | Crystallization and preliminary X-ray analysis of a domain in the Runx2 transcription factor that interacts with the 1alpha,25 dihydroxy vitamin D3 receptor |
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