Cryo-EM structure of his-elemental paused elongation complex with an unfolded TL (2)

An ensemble of interconverting conformations of the elemental paused transcription complex creates regulatory options.

Entry contains improper nucleotide linkages.

Entry contains numerous improper peptide linkages.

An RNA polymerase elongation complex was assembled at the weak elemental pausing site derived from his-pause sequence.

DNA-directed RNA polymerase subunit alpha

DNA-directed RNA polymerase subunit beta

DNA-directed RNA polymerase subunit beta'

DNA-directed RNA polymerase subunit omega

RNAP subunit alpha,RNA polymerase subunit alpha,Transcriptase subunit alpha

RNAP subunit beta,RNA polymerase subunit beta,Transcriptase subunit beta

RNAP subunit beta',RNA polymerase subunit beta',Transcriptase subunit beta'

RNAP omega subunit,RNA polymerase omega subunit,Transcriptase subunit omega

National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)

a gel filtration chromatography combined with SDS-PAGE confirmed the presence of all the RNA polymerase subunits
RNA polymerase, cryo-EM structure, elemental pause, Escherichia coli, transcription, TRANSFERASE-DNA-RNA complex, transcriptional regulation, transcriptional pausing