RNA polymerase I: a multifunctional molecular machine.
In this issue, Kuhn et al. (2007) report the complete structure of the 14-subunit yeast RNA polymerase (Pol) I enzyme at 12 A resolution using cryo-electron microscopy (cryo-EM). Their study reveals that three subunits of Pol I perform functions in transcription elongation that are outsourced to the transcription factors TFIIF and TFIIS in the analogous Pol II transcription system.
Haag
Jeremy R
JR
Department of Biology, Washington University, 1 Brookings Drive, St. Louis, MO, USA.
Pikaard
Craig S
CS
D001665:Binding Sites; D004256:DNA Polymerase I / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D008958:Models, Molecular; D009154:Mutation; D010445:Peptide Elongation Factors / Q000737:chemistry / Q000378:metabolism; D010448:Peptide Initiation Factors / Q000737:chemistry / Q000378:metabolism; D011401:Promoter Regions, Genetic; D011487:Protein Conformation; D054730:Protein Interaction Domains and Motifs; D017434:Protein Structure, Tertiary; D021122:Protein Subunits; D012323:RNA Processing, Post-Transcriptional; D012335:RNA, Ribosomal / Q000235:genetics / Q000378:metabolism*; D012441:Saccharomyces cerevisiae / Q000201:enzymology* / Q000235:genetics; D029701:Saccharomyces cerevisiae Proteins / Q000737:chemistry* / Q000235:genetics / Q000378:metabolism; D013329:Structure-Activity Relationship; D019473:Transcription Factors, TFII / Q000737:chemistry / Q000378:metabolism; D014158:Transcription, Genetic; D035602:Transcriptional Elongation Factors / Q000737:chemistry / Q000378:metabolism
D010445:Peptide Elongation Factors; D010448:Peptide Initiation Factors; D021122:Protein Subunits; D012335:RNA, Ribosomal; D029701:Saccharomyces cerevisiae Proteins; D019473:Transcription Factors, TFII; D035602:Transcriptional Elongation Factors; C018648:transcription factor S-II; D004256:DNA Polymerase I; C083536:POL1 protein, S cerevisiae; C056604:transcription factor TFIIF