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TitleRNA polymerase and transcription elongation factor Spt4/5 complex structure.
Journal, issue, pagesProc Natl Acad Sci U S A, Vol. 108, Issue 2, Page 546-550, Year 2011
Publish dateJan 11, 2011
AuthorsBrianna J Klein / Daniel Bose / Kevin J Baker / Zahirah M Yusoff / Xiaodong Zhang / Katsuhiko S Murakami /
PubMed AbstractSpt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in ...Spt4/5 in archaea and eukaryote and its bacterial homolog NusG is the only elongation factor conserved in all three domains of life and plays many key roles in cotranscriptional regulation and in recruiting other factors to the elongating RNA polymerase. Here, we present the crystal structure of Spt4/5 as well as the structure of RNA polymerase-Spt4/5 complex using cryoelectron microscopy reconstruction and single particle analysis. The Spt4/5 binds in the middle of RNA polymerase claw and encloses the DNA, reminiscent of the DNA polymerase clamp and ring helicases. The transcription elongation complex model reveals that the Spt4/5 is an upstream DNA holder and contacts the nontemplate DNA in the transcription bubble. These structures reveal that the cellular RNA polymerases also use a strategy of encircling DNA to enhance its processivity as commonly observed for many nucleic acid processing enzymes including DNA polymerases and helicases.
External linksProc Natl Acad Sci U S A / PubMed:21187417 / PubMed Central
MethodsEM (single particle) / X-ray diffraction
Resolution1.8 - 13.0 Å
Structure data

EMDB-1840:
The RNA polymerase and transcription elongation factor Spt4-5 complex structure
Method: EM (single particle) / Resolution: 13.0 Å

PDB-3p8b:
X-ray crystal structure of Pyrococcus furiosus transcription elongation factor Spt4/5
Method: X-RAY DIFFRACTION / Resolution: 1.8 Å

Chemicals

ChemComp-ZN:
Unknown entry

ChemComp-BME:
BETA-MERCAPTOETHANOL

ChemComp-GOL:
GLYCEROL

ChemComp-HOH:
WATER

Source
  • pyrococcus furiosus (archaea)
KeywordsTRANSFERASE/TRANSCRIPTION / transcription elongation factor / RNA polymerase / TRANSFERASE-TRANSCRIPTION complex

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