Purification of a high-mobility-group 1 sea-urchin protein and cloning of cDNAs
The isolation of the sea urchin high-mobility-group 1 (HMG1) protein, the cloning of corresponding cDNA clones and the similarity to the human homologue are described. Sea urchin HMG1 was purified as one of the nuclear embryonic proteins which associate with an upstream regulatory element (El) of th...
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| Veröffentlicht in: | Gene 1995-10, Vol.164 (2), p.211-218 |
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| creator | Niemeyer, Christina C. Foerster-Ziober, Amy Flytzanis, Constantin N. |
| description | The isolation of the sea urchin high-mobility-group 1 (HMG1) protein, the cloning of corresponding cDNA clones and the similarity to the human homologue are described. Sea urchin HMG1 was purified as one of the nuclear embryonic proteins which associate with an upstream regulatory element
(El) of the
Strongylocentrotus purpuratus (Sp) CyIIIb actin-encoding gene. Using a synthetic oligodeoxyribonucleotide (oligo) which includes the
E1 cis-acting element in a DNA affinity chromatography purification, the most prominent of the binding proteins was isolated and the N terminus sequenced. cDNA clones were isolated by screening an embryonic cDNA library with a synthetic oligo derived from the amino acid (aa) sequence. Comparison of the cDNAs ORF to known proteins revealed a 50% aa identity to the mammalian HMG1 and all the structural characteristics of this group of proteins. The sea urchin protein, SpHMG1, was synthesized in bacteria, as well as translated in vitro. Binding assays carried out with the recombinant SpHMG1 protein did not produce specific in vitro complexes with
E1. |
| doi_str_mv | 10.1016/0378-1119(95)00410-8 |
| format | Article |
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(El) of the
Strongylocentrotus purpuratus (Sp) CyIIIb actin-encoding gene. Using a synthetic oligodeoxyribonucleotide (oligo) which includes the
E1 cis-acting element in a DNA affinity chromatography purification, the most prominent of the binding proteins was isolated and the N terminus sequenced. cDNA clones were isolated by screening an embryonic cDNA library with a synthetic oligo derived from the amino acid (aa) sequence. Comparison of the cDNAs ORF to known proteins revealed a 50% aa identity to the mammalian HMG1 and all the structural characteristics of this group of proteins. The sea urchin protein, SpHMG1, was synthesized in bacteria, as well as translated in vitro. Binding assays carried out with the recombinant SpHMG1 protein did not produce specific in vitro complexes with
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(El) of the
Strongylocentrotus purpuratus (Sp) CyIIIb actin-encoding gene. Using a synthetic oligodeoxyribonucleotide (oligo) which includes the
E1 cis-acting element in a DNA affinity chromatography purification, the most prominent of the binding proteins was isolated and the N terminus sequenced. cDNA clones were isolated by screening an embryonic cDNA library with a synthetic oligo derived from the amino acid (aa) sequence. Comparison of the cDNAs ORF to known proteins revealed a 50% aa identity to the mammalian HMG1 and all the structural characteristics of this group of proteins. The sea urchin protein, SpHMG1, was synthesized in bacteria, as well as translated in vitro. Binding assays carried out with the recombinant SpHMG1 protein did not produce specific in vitro complexes with
E1.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Base Sequence</subject><subject>cDNA isolation</subject><subject>Cloning, Molecular - methods</subject><subject>conserved motif</subject><subject>DNA, Complementary - biosynthesis</subject><subject>DNA, Complementary - isolation & purification</subject><subject>Echinodermata</subject><subject>Echinoidea</subject><subject>High Mobility Group Proteins - biosynthesis</subject><subject>High Mobility Group Proteins - genetics</subject><subject>High Mobility Group Proteins - isolation & purification</subject><subject>Humans</subject><subject>Mammals</subject><subject>Marine</subject><subject>Molecular Sequence Data</subject><subject>Open Reading Frames</subject><subject>Protein Biosynthesis</subject><subject>Protein purification</subject><subject>Rabbits</subject><subject>recombinant protein production</subject><subject>Restriction Mapping</subject><subject>Reticulocytes - metabolism</subject><subject>Sea Urchins - genetics</subject><subject>Sea Urchins - metabolism</subject><subject>Sequence Homology, Amino Acid</subject><subject>Strongylocentrotus purpuratus</subject><issn>0378-1119</issn><issn>1879-0038</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNqFkEtPwzAQhC0EgvL4ByDlhOBg8MZxYl-QKt4SAg7cLcfetEZpXOwEiX9PSiuOsJc57Mzs6iPkGNgFMCgvGa8kBQB1psQ5YwUwKrfIBGSlKGNcbpPJr2WP7Kf0zsYRIt8lu5VQjHM-IS-vQ_SNt6b3octCk5ls7mdzugi1b33_RWcxDMsMsoSGDtHOfZctY-hxVNO5zLah891slbQ3z9N0SHYa0yY82ugBebu7fbt-oE8v94_X0ydquZQ9tYW03JbO5BVTjikLyjWKF5a5piwKU3BX19KUxioBDg3k2NQVQKGQo-L8gJyua8dfPgZMvV74ZLFtTYdhSLqqylKAyv81QsVywUCMxmJttDGkFLHRy-gXJn5pYHrFW69g6hVMrYT-4a3lGDvZ9A_1At1vaAN43F-t9zjC-PQYdbIeO4vOR7S9dsH_feAb2PWOVQ</recordid><startdate>19951027</startdate><enddate>19951027</enddate><creator>Niemeyer, Christina C.</creator><creator>Foerster-Ziober, Amy</creator><creator>Flytzanis, Constantin N.</creator><general>Elsevier 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>7TM</scope><scope>8FD</scope><scope>F1W</scope><scope>FR3</scope><scope>H95</scope><scope>H99</scope><scope>L.F</scope><scope>L.G</scope><scope>P64</scope><scope>7X8</scope></search><sort><creationdate>19951027</creationdate><title>Purification of a high-mobility-group 1 sea-urchin protein and cloning of cDNAs</title><author>Niemeyer, Christina C. ; 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Sea urchin HMG1 was purified as one of the nuclear embryonic proteins which associate with an upstream regulatory element
(El) of the
Strongylocentrotus purpuratus (Sp) CyIIIb actin-encoding gene. Using a synthetic oligodeoxyribonucleotide (oligo) which includes the
E1 cis-acting element in a DNA affinity chromatography purification, the most prominent of the binding proteins was isolated and the N terminus sequenced. cDNA clones were isolated by screening an embryonic cDNA library with a synthetic oligo derived from the amino acid (aa) sequence. Comparison of the cDNAs ORF to known proteins revealed a 50% aa identity to the mammalian HMG1 and all the structural characteristics of this group of proteins. The sea urchin protein, SpHMG1, was synthesized in bacteria, as well as translated in vitro. Binding assays carried out with the recombinant SpHMG1 protein did not produce specific in vitro complexes with
E1.</abstract><cop>Netherlands</cop><pub>Elsevier B.V</pub><pmid>7590333</pmid><doi>10.1016/0378-1119(95)00410-8</doi><tpages>8</tpages></addata></record> |
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| ispartof | Gene, 1995-10, Vol.164 (2), p.211-218 |
| issn | 0378-1119 1879-0038 |
| language | eng |
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| source | MEDLINE; Elsevier ScienceDirect Journals Complete |
| subjects | Amino Acid Sequence Animals Base Sequence cDNA isolation Cloning, Molecular - methods conserved motif DNA, Complementary - biosynthesis DNA, Complementary - isolation & purification Echinodermata Echinoidea High Mobility Group Proteins - biosynthesis High Mobility Group Proteins - genetics High Mobility Group Proteins - isolation & purification Humans Mammals Marine Molecular Sequence Data Open Reading Frames Protein Biosynthesis Protein purification Rabbits recombinant protein production Restriction Mapping Reticulocytes - metabolism Sea Urchins - genetics Sea Urchins - metabolism Sequence Homology, Amino Acid Strongylocentrotus purpuratus |
| title | Purification of a high-mobility-group 1 sea-urchin protein and cloning of cDNAs |
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