Purification and characterization of the arylphorin gene specific binding protein from an embryonic cell line of Sarcophaga peregrina (flesh fly)
Previously, we purified a DNA binding protein from a nuclear extract of the fat body of Sarcophaga peregrina larvae that binds to the ACCACAACA motif in the 5'-upstream region of the arylphorin gene, and suggested that this protein is a transcriptional activator of the arylphorin gene. In this...
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| Veröffentlicht in: | Journal of biochemistry (Tokyo) 1993-07, Vol.114 (1), p.55-60 |
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| container_title | Journal of biochemistry (Tokyo) |
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| creator | Adachi, N Kubo, T Natori, S |
| description | Previously, we purified a DNA binding protein from a nuclear extract of the fat body of Sarcophaga peregrina larvae that binds to the ACCACAACA motif in the 5'-upstream region of the arylphorin gene, and suggested that this protein is a transcriptional activator of the arylphorin gene. In this study, we detected and purified the same protein (ABP-1) from an embryonic cell line of Sarcophaga that does not express the arylphorin gene. Unlike the fat body, which synthesizes arylphorin actively, the embryonic cells were found to contain an additional DNA binding protein (ABP-2) that bound to the same DNA probe as ABP-1, suggesting a novel mechanism of regulation of the arylphorin gene. |
| doi_str_mv | 10.1093/oxfordjournals.jbchem.a124140 |
| format | Article |
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In this study, we detected and purified the same protein (ABP-1) from an embryonic cell line of Sarcophaga that does not express the arylphorin gene. 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Kubo, T ; Natori, S</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-f341t-7637405d68ab512d755f06d77c1cd0de2ff1f5d7d45e76dd244b133b06f9017d3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1993</creationdate><topic>Animals</topic><topic>Base Sequence</topic><topic>Binding Sites</topic><topic>Cell Line</topic><topic>cell lines</topic><topic>Chromatography, Affinity</topic><topic>Diptera - genetics</topic><topic>Diptera - metabolism</topic><topic>DNA - genetics</topic><topic>DNA - metabolism</topic><topic>DNA Probes</topic><topic>DNA-binding proteins</topic><topic>DNA-Binding Proteins - chemistry</topic><topic>DNA-Binding Proteins - isolation & purification</topic><topic>DNA-Binding Proteins - metabolism</topic><topic>Electrophoresis, Polyacrylamide Gel</topic><topic>embryo (animal)</topic><topic>Glycoproteins - chemistry</topic><topic>Glycoproteins - genetics</topic><topic>inhibition</topic><topic>Insect Hormones - chemistry</topic><topic>Insect Hormones - genetics</topic><topic>Insect Proteins</topic><topic>Mice</topic><topic>Molecular Sequence Data</topic><topic>purification</topic><topic>Sarcophaga peregrina</topic><topic>transcription (genetics)</topic><topic>Transcription, Genetic</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Adachi, N</creatorcontrib><creatorcontrib>Kubo, T</creatorcontrib><creatorcontrib>Natori, S</creatorcontrib><collection>AGRIS</collection><collection>Istex</collection><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 biochemistry (Tokyo)</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Adachi, N</au><au>Kubo, T</au><au>Natori, S</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Purification and characterization of the arylphorin gene specific binding protein from an embryonic cell line of Sarcophaga peregrina (flesh fly)</atitle><jtitle>Journal of biochemistry (Tokyo)</jtitle><addtitle>J Biochem</addtitle><date>1993-07-01</date><risdate>1993</risdate><volume>114</volume><issue>1</issue><spage>55</spage><epage>60</epage><pages>55-60</pages><issn>0021-924X</issn><eissn>1756-2651</eissn><abstract>Previously, we purified a DNA binding protein from a nuclear extract of the fat body of Sarcophaga peregrina larvae that binds to the ACCACAACA motif in the 5'-upstream region of the arylphorin gene, and suggested that this protein is a transcriptional activator of the arylphorin gene. In this study, we detected and purified the same protein (ABP-1) from an embryonic cell line of Sarcophaga that does not express the arylphorin gene. Unlike the fat body, which synthesizes arylphorin actively, the embryonic cells were found to contain an additional DNA binding protein (ABP-2) that bound to the same DNA probe as ABP-1, suggesting a novel mechanism of regulation of the arylphorin gene.</abstract><cop>England</cop><pub>Oxford University Press</pub><pmid>8407877</pmid><doi>10.1093/oxfordjournals.jbchem.a124140</doi><tpages>6</tpages></addata></record> |
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| ispartof | Journal of biochemistry (Tokyo), 1993-07, Vol.114 (1), p.55-60 |
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| language | eng |
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| source | J-STAGE Free; MEDLINE; Oxford University Press Journals Digital Archive Legacy; Free Full-Text Journals in Chemistry |
| subjects | Animals Base Sequence Binding Sites Cell Line cell lines Chromatography, Affinity Diptera - genetics Diptera - metabolism DNA - genetics DNA - metabolism DNA Probes DNA-binding proteins DNA-Binding Proteins - chemistry DNA-Binding Proteins - isolation & purification DNA-Binding Proteins - metabolism Electrophoresis, Polyacrylamide Gel embryo (animal) Glycoproteins - chemistry Glycoproteins - genetics inhibition Insect Hormones - chemistry Insect Hormones - genetics Insect Proteins Mice Molecular Sequence Data purification Sarcophaga peregrina transcription (genetics) Transcription, Genetic |
| title | Purification and characterization of the arylphorin gene specific binding protein from an embryonic cell line of Sarcophaga peregrina (flesh fly) |
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