Structure-function studies of the RNA polymerase II elongation complex

被引:31
|
作者
Brueckner, Florian
Armache, Karim-Jean
Cheung, Alan
Damsma, Gerke E.
Kettenberger, Hubert
Lehmann, Elisabeth
Sydow, Jasmin
Cramer, Patrick [1 ]
机构
[1] Univ Munich, Gene Ctr Munich, D-81377 Munich, Germany
来源
ACTA CRYSTALLOGRAPHICA SECTION D-STRUCTURAL BIOLOGY | 2009年 / 65卷
关键词
CYCLOBUTANE PYRIMIDINE DIMER; TRANSCRIPTION-COUPLED REPAIR; NUCLEOTIDE EXCISION-REPAIR; CISPLATIN-DAMAGED DNA; SYN THYMINE DIMER; ANGSTROM RESOLUTION; CRYSTAL-STRUCTURE; ALPHA-AMANITIN; TRIGGER LOOP; RECOGNITION;
D O I
10.1107/S0907444908039875
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
RNA polymerase II (Pol II) is the eukaryotic enzyme that is responsible for transcribing all protein-coding genes into messenger RNA ( mRNA). The mRNA-transcription cycle can be divided into three stages: initiation, elongation and termination. During elongation, Pol II moves along a DNA template and synthesizes a complementary RNA chain in a processive manner. X-ray structural analysis has proved to be a potent tool for elucidating the mechanism of Pol II elongation. Crystallographic snapshots of different functional states of the Pol II elongation complex (EC) have elucidated mechanistic details of nucleotide addition and Pol II translocation. Further structural studies in combination with in vitro transcription experiments led to a mechanistic understanding of various additional features of the EC, including its inhibition by the fungal toxin alpha-amanitin, the tunability of the active site by the elongation factor TFIIS, the recognition of DNA lesions and the use of RNA as a template.
引用
收藏
页码:112 / 120
页数:9
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