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3H3V

Yeast RNAP II containing poly(A)-signal sequence in the active site

Summary for 3H3V
Entry DOI10.2210/pdb3h3v/pdb
DescriptorDNA-directed RNA polymerase II subunit RPB1, DNA-directed RNA polymerases I, II, and III subunit RPABC5, DNA-directed RNA polymerase II subunit RPB11, ... (17 entities in total)
Functional Keywordstransferase/dna/rna, dna-binding, phosphorylation, rna polymerase ii, metal-binding, nuclear protein, transcription bubble, elongation complex, transferase, transcription, polyadenylation, termination, dna-directed rna polymerase, isopeptide bond, magnesium, nucleotidyltransferase, nucleus, phosphoprotein, zinc-finger, dna damage, dna repair, mrna processing, transferase-dna-rna complex
Biological sourceSaccharomyces cerevisiae (yeast)
More
Cellular locationNucleus: P04050 P38902 P08518 P16370 P20433 P20434 P34087 P20436
Nucleus, nucleolus : P22139 P40422 P27999
Cytoplasm : P20435
Total number of polymer chains15
Total formula weight531996.79
Authors
Dengl, S.,Cramer, P. (deposition date: 2009-04-17, release date: 2009-06-16, Last modification date: 2023-09-06)
Primary citationDengl, S.,Cramer, P.
Torpedo Nuclease Rat1 Is Insufficient to Terminate RNA Polymerase II in Vitro
J.Biol.Chem., 284:21270-21279, 2009
Cited by
PubMed Abstract: Termination of RNA polymerase (pol) II transcription in vivo requires the 5'-RNA exonuclease Rat1. It was proposed that Rat1 degrades RNA from the 5'-end that is created by transcript cleavage, catches up with elongating pol II, and acts like a Torpedo that removes pol II from DNA. Here we test the Torpedo model in an in vitro system based on bead-coupled pol II elongation complexes (ECs). Recombinant Rat1 complexes with Rai1, and with Rai1 and Rtt103, degrade RNA extending from the EC until they reach the polymerase surface but fail to terminate pol II. Instead, the EC retains an approximately 18-nucleotide RNA that remains with its 3'-end at the active site and can be elongated. Thus, pol II termination apparently requires a factor or several factors in addition to Rat1, Rai1, and Rtt103, post-translational modifications of these factors, or unusual reaction conditions.
PubMed: 19535338
DOI: 10.1074/jbc.M109.013847
PDB entries with the same primary citation
Experimental method
X-RAY DIFFRACTION (4 Å)
Structure validation

226707

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