Characterization of the Calf Thymus Hairpin-binding Factor Involved in Histone Pre-mRNA 3â² End Processing
Using ion exchange chromatography we have enriched the RNA hairpin-binding factor involved in histone pre-mRNA processing from calf thymus whole cell extract. We demonstrate that the interaction of the factor with its target RNA sequence, the hairpin structure located at the 3â² end of mature histo...
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| Veröffentlicht in: | The Journal of biological chemistry 1997-04, Vol.272 (16), p.10435 |
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| container_title | The Journal of biological chemistry |
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| creator | André Schaller Franck Martin Berndt Müller |
| description | Using ion exchange chromatography we have enriched the RNA hairpin-binding factor involved in histone pre-mRNA processing
from calf thymus whole cell extract. We demonstrate that the interaction of the factor with its target RNA sequence, the hairpin
structure located at the 3â² end of mature histone mRNA, is sequence-specific and highly salt-resistant. We have developed
a simple in vitro system which allows detection of activities stimulating histone pre-mRNA 3â² end processing, based on mouse cell nuclear extract
fractionated by Mono Q column chromatography. Using this system, we show that the bovine hairpin-binding factor participates
in histone pre-mRNA 3Ⲡend processing in vitro . We have further purified the hairpin-binding factor in form of a RNA·protein complex by RNA-mediated elution from phosphocellulose.
This led to a fraction highly enriched for 2 proteins of 40 and 43 kDa. |
| doi_str_mv | 10.1074/jbc.272.16.10435 |
| format | Article |
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from calf thymus whole cell extract. We demonstrate that the interaction of the factor with its target RNA sequence, the hairpin
structure located at the 3â² end of mature histone mRNA, is sequence-specific and highly salt-resistant. We have developed
a simple in vitro system which allows detection of activities stimulating histone pre-mRNA 3â² end processing, based on mouse cell nuclear extract
fractionated by Mono Q column chromatography. Using this system, we show that the bovine hairpin-binding factor participates
in histone pre-mRNA 3Ⲡend processing in vitro . We have further purified the hairpin-binding factor in form of a RNA·protein complex by RNA-mediated elution from phosphocellulose.
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from calf thymus whole cell extract. We demonstrate that the interaction of the factor with its target RNA sequence, the hairpin
structure located at the 3â² end of mature histone mRNA, is sequence-specific and highly salt-resistant. We have developed
a simple in vitro system which allows detection of activities stimulating histone pre-mRNA 3â² end processing, based on mouse cell nuclear extract
fractionated by Mono Q column chromatography. Using this system, we show that the bovine hairpin-binding factor participates
in histone pre-mRNA 3Ⲡend processing in vitro . We have further purified the hairpin-binding factor in form of a RNA·protein complex by RNA-mediated elution from phosphocellulose.
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from calf thymus whole cell extract. We demonstrate that the interaction of the factor with its target RNA sequence, the hairpin
structure located at the 3â² end of mature histone mRNA, is sequence-specific and highly salt-resistant. We have developed
a simple in vitro system which allows detection of activities stimulating histone pre-mRNA 3â² end processing, based on mouse cell nuclear extract
fractionated by Mono Q column chromatography. Using this system, we show that the bovine hairpin-binding factor participates
in histone pre-mRNA 3Ⲡend processing in vitro . We have further purified the hairpin-binding factor in form of a RNA·protein complex by RNA-mediated elution from phosphocellulose.
This led to a fraction highly enriched for 2 proteins of 40 and 43 kDa.</abstract><pub>American Society for Biochemistry and Molecular Biology</pub><pmid>9099685</pmid><doi>10.1074/jbc.272.16.10435</doi></addata></record> |
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| ispartof | The Journal of biological chemistry, 1997-04, Vol.272 (16), p.10435 |
| issn | 0021-9258 1083-351X |
| language | eng |
| recordid | cdi_highwire_biochem_272_16_10435 |
| source | Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; Alma/SFX Local Collection |
| title | Characterization of the Calf Thymus Hairpin-binding Factor Involved in Histone Pre-mRNA 3â² End Processing |
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