Architecture of the RNA polymerase II-TFIIS complex and implications for mRNA cleavage

被引:282
作者
Kettenberger, H [1 ]
Armache, KJ [1 ]
Cramer, P [1 ]
机构
[1] Univ Munich, Inst Biochem, Gene Ctr, D-81377 Munich, Germany
关键词
D O I
10.1016/S0092-8674(03)00598-1
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
The transcription elongation factor TFIIS induces mRNA cleavage by enhancing the intrinsic nuclease activity of RNA polymerase (Pol) II. We have diffused TFIIS into Pol II crystals and derived a model of the Pol II-TFIIS complex from X-ray diffraction data to 3.8 Angstrom resolution. TFIIS extends from the polymerase surface via a pore to the internal active site, spanning a distance of 100 Angstrom. Two essential and invariant acidic residues in a TFIIS loop complement the Pol II active site and could position a metal ion and a water molecule for hydrolytic RNA cleavage. TFIIS also induces extensive structural changes in Pol II that would realign nucleic acids in the active center. Our results support the idea that Pol II contains a single tunable active site for RNA polymerization and cleavage, in contrast to DNA polymerases with two separate active sites for DNA polymerization and cleavage.
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收藏
页码:347 / 357
页数:11
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