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Structural basis of RNA polymerase II substrate specificity and catalysis
Author(s) -
Wang Dong,
Bushnell David A.,
Westover Kenneth D.,
Kaplan Craig D.,
Kornberg Roger D.
Publication year - 2007
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.21.5.a656-c
Subject(s) - phosphodiester bond , polymerase , transcription (linguistics) , chemistry , nucleotide , rna polymerase , rna polymerase ii , biochemistry , rna , microbiology and biotechnology , stereochemistry , biophysics , biology , dna , gene , gene expression , linguistics , promoter , philosophy
The fundamental mechanism of transcription is conserved among cellular RNA polymerases. New structures of RNA polymerase II (pol II) transcribing complexes reveal a likely key to transcription. A flexible structural element swings beneath a correct nucleoside triphosphate (NTP) in the nucleotide addition site, closing off the active center, and forming an extensive network of interactions with the NTP base, sugar, phosphates, and additional pol II residues. A histidine side chain in this element, precisely positioned by these interactions, may facilitate phosphodiester bond formation. Recognition and catalysis are thus coupled, ensuring the fidelity of transcription of pol II.