Characterization of the calf thymus hairpin-binding factor involved in histone pre-mRNA 3' end processing

被引：0

作者：

Schaller, A ^{[1
]}

Martin, F ^{[1
]}

Muller, B ^{[1
]}

机构：

[1] UNIV BERN,ABT ENTWICKLUNGSBIOL,INST ZOOL,CH-3012 BERN,SWITZERLAND

来源：

JOURNAL OF BIOLOGICAL CHEMISTRY | 1997年 / 272卷 / 16期

关键词：

D O I：

暂无

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

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 3' 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 3' 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 3' end 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.

引用

页码：10435 / 10441

页数：7

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