The nuclear 42-kDa phosphoprotein preferentially binds promoter-containing single-stranded DNA
The DNA-binding activity of a 42-kDa phosphoprotein from salivary gland cells and cultured epithelial cells of Chironomus tentans have been analyzed by the Southwestern technique. Both the salivary gland and the epithelial cell 42-kDa polypeptides were found to be single-stranded DNA-binding protein...
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| Veröffentlicht in: | Biochemical and biophysical research communications 1991-05, Vol.176 (3), p.1565-1570 |
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| creator | Stigare, J. Egyhazi, E. |
| description | The DNA-binding activity of a 42-kDa phosphoprotein from salivary gland cells and cultured epithelial cells of
Chironomus tentans have been analyzed by the Southwestern technique. Both the salivary gland and the epithelial cell 42-kDa polypeptides were found to be single-stranded DNA-binding proteins. They bind to single-stranded promoter-containing restriction fragments including sequences from −204 to +74 from the ecdysterone controlled I-18C gene as well as sequences including the joint histone
H2A
H2B
promoters in a sequence selective manner. By contrast, the 42-kDa polypeptides show no significant binding to intragenic restriction fragments from +71 to +351 from the I-18C gene. Previous and present data taken together suggest that the 42-kDa protein has a general role in the regulation of protein coding genes. |
| doi_str_mv | 10.1016/0006-291X(91)90466-K |
| format | Article |
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Chironomus tentans have been analyzed by the Southwestern technique. Both the salivary gland and the epithelial cell 42-kDa polypeptides were found to be single-stranded DNA-binding proteins. They bind to single-stranded promoter-containing restriction fragments including sequences from −204 to +74 from the ecdysterone controlled I-18C gene as well as sequences including the joint histone
H2A
H2B
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Chironomus tentans have been analyzed by the Southwestern technique. Both the salivary gland and the epithelial cell 42-kDa polypeptides were found to be single-stranded DNA-binding proteins. They bind to single-stranded promoter-containing restriction fragments including sequences from −204 to +74 from the ecdysterone controlled I-18C gene as well as sequences including the joint histone
H2A
H2B
promoters in a sequence selective manner. By contrast, the 42-kDa polypeptides show no significant binding to intragenic restriction fragments from +71 to +351 from the I-18C gene. Previous and present data taken together suggest that the 42-kDa protein has a general role in the regulation of protein coding genes.</description><subject>Analytical, structural and metabolic biochemistry</subject><subject>Animals</subject><subject>Biological and medical sciences</subject><subject>Cell Nucleus - metabolism</subject><subject>Cells, Cultured</subject><subject>Chironomidae</subject><subject>Diptera</subject><subject>DNA Probes</subject><subject>DNA, Single-Stranded - metabolism</subject><subject>DNA-Binding Proteins - isolation & purification</subject><subject>DNA-Binding Proteins - metabolism</subject><subject>Epithelium - metabolism</subject><subject>Fundamental and applied biological sciences. Psychology</subject><subject>Holoproteins</subject><subject>Immunoblotting</subject><subject>Molecular Weight</subject><subject>Nuclear proteins</subject><subject>Nuclear Proteins - isolation & purification</subject><subject>Nuclear Proteins - metabolism</subject><subject>Phosphoproteins - isolation & purification</subject><subject>Phosphoproteins - metabolism</subject><subject>Promoter Regions, Genetic</subject><subject>Proteins</subject><subject>Salivary Glands - metabolism</subject><issn>0006-291X</issn><issn>1090-2104</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1991</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkE1v1DAQhi1EVZbCPwApFyo4GGYcx4kvSFU_oGpFL63ECWvqTKgh6yx2tlL_PV52VW5wsC35febV6BHiFcJ7BDQfAMBIZfHrW4vvLGhj5MUTsUCwIBWCfioWj8gz8TznHwCI2th9sa-gtk0NC_Ht-o6ruPYjU6q0kj9PqFrdTbmcVZpmDrFaJR44cZwDjeNDdRtin8vntCxxkn6KM4UY4vcql2tkmedEsee-Ovly9ELsDTRmfrl7D8TN2en18Wd5efXp_PjoUnqN3SxbA7a1nqFVirRlMAoG7O1giRgbZeqWqNGDx65rVd1yM9QdAtmu8aSQ6gNxuO0te_1ac57dMmTP40iRp3V2HTS2yND_BdEg1rruCqi3oE9TzkWBW6WwpPTgENzGv9vIdRu5zqL7499dlLHXu_717ZL7x6Gd8JK_2eWUPY1DUeVD_ttt2w60tYX7uOW4WLsPnFz2gaPnPiT2s-un8O9FfgNwAKFf</recordid><startdate>19910515</startdate><enddate>19910515</enddate><creator>Stigare, J.</creator><creator>Egyhazi, E.</creator><general>Elsevier Inc</general><general>Elsevier</general><scope>IQODW</scope><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>7SS</scope><scope>7TM</scope><scope>7X8</scope></search><sort><creationdate>19910515</creationdate><title>The nuclear 42-kDa phosphoprotein preferentially binds promoter-containing single-stranded DNA</title><author>Stigare, J. ; Egyhazi, E.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c418t-760979ce0722a49e0620f1d9f9aae152637aa54fc1887237e5f3810a985ca21a3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1991</creationdate><topic>Analytical, structural and metabolic biochemistry</topic><topic>Animals</topic><topic>Biological and medical sciences</topic><topic>Cell Nucleus - metabolism</topic><topic>Cells, Cultured</topic><topic>Chironomidae</topic><topic>Diptera</topic><topic>DNA Probes</topic><topic>DNA, Single-Stranded - metabolism</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Epithelium - metabolism</topic><topic>Fundamental and applied biological sciences. Psychology</topic><topic>Holoproteins</topic><topic>Immunoblotting</topic><topic>Molecular Weight</topic><topic>Nuclear proteins</topic><topic>Nuclear Proteins - isolation & purification</topic><topic>Nuclear Proteins - metabolism</topic><topic>Phosphoproteins - isolation & purification</topic><topic>Phosphoproteins - metabolism</topic><topic>Promoter Regions, Genetic</topic><topic>Proteins</topic><topic>Salivary Glands - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Stigare, J.</creatorcontrib><creatorcontrib>Egyhazi, E.</creatorcontrib><collection>Pascal-Francis</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Nucleic Acids Abstracts</collection><collection>MEDLINE - Academic</collection><jtitle>Biochemical and biophysical research communications</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Stigare, J.</au><au>Egyhazi, E.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>The nuclear 42-kDa phosphoprotein preferentially binds promoter-containing single-stranded DNA</atitle><jtitle>Biochemical and biophysical research communications</jtitle><addtitle>Biochem Biophys Res Commun</addtitle><date>1991-05-15</date><risdate>1991</risdate><volume>176</volume><issue>3</issue><spage>1565</spage><epage>1570</epage><pages>1565-1570</pages><issn>0006-291X</issn><eissn>1090-2104</eissn><coden>BBRCA9</coden><abstract>The DNA-binding activity of a 42-kDa phosphoprotein from salivary gland cells and cultured epithelial cells of
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H2A
H2B
promoters in a sequence selective manner. By contrast, the 42-kDa polypeptides show no significant binding to intragenic restriction fragments from +71 to +351 from the I-18C gene. Previous and present data taken together suggest that the 42-kDa protein has a general role in the regulation of protein coding genes.</abstract><cop>San Diego, CA</cop><pub>Elsevier Inc</pub><pmid>2039530</pmid><doi>10.1016/0006-291X(91)90466-K</doi><tpages>6</tpages></addata></record> |
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| ispartof | Biochemical and biophysical research communications, 1991-05, Vol.176 (3), p.1565-1570 |
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| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals |
| subjects | Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Nucleus - metabolism Cells, Cultured Chironomidae Diptera DNA Probes DNA, Single-Stranded - metabolism DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Epithelium - metabolism Fundamental and applied biological sciences. Psychology Holoproteins Immunoblotting Molecular Weight Nuclear proteins Nuclear Proteins - isolation & purification Nuclear Proteins - metabolism Phosphoproteins - isolation & purification Phosphoproteins - metabolism Promoter Regions, Genetic Proteins Salivary Glands - metabolism |
| title | The nuclear 42-kDa phosphoprotein preferentially binds promoter-containing single-stranded DNA |
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