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The HelD N-terminal domain inserts into the RNAP secondary channel; domains

The HelD N-terminal domain inserts into the RNAP secondary channel; domains

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Figure 2: The HelD N-terminal domain inserts into the RNAP secondary...
Figure 4: Binding of Msm HelD to RNAP and its effects on DNA-RNAP...
Figure 5: Schematic diagram of HelD function in RNAP recycling.
Mycobacterial HelD is a nucleic acids-clearing factor for RNA polymerase
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  • Jul 2020
RNA synthesis is central to life, and RNA polymerase depends on accessory factors for recovery from stalled states and adaption to environmental changes. Here we investigated the mechanism by which a helicase-like factor HelD recycles RNA polymerase. We report a cryo-EM structure of an unprecedented complex between the Mycobacterium smegmatis RNA p...
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Context 1
... reconstituted a complex of Msm RNAP core and Msm HelD from purified 78 recombinant proteins ( Figure S2), and froze an isolated homogenous fraction of the complex 79 on cryo-EM grids. We collected multiple preliminary cryo-EM datasets, which allowed us to 80 optimize the cryo-EM conditions for high-resolution three-dimensional (3D) single-particle the RNAP core. ...
Context 2
... 1A-2A heterodimer establishes the canonical tertiary structure to form an NTP-176 binding pocket. Conserved residues of motifs Q, I, II, ~III, IIIa, Va, and VI are then likely involved 177 in ATP binding 7,18 (Figure 2d) while motifs and residues typical for DNA binding are missing. ...
Context 3
... /2020 towards a pyrimidine-containing counterpart (Figure 2e, S7f). We also added ATP or non-182 hydrolysable ATP analogue to the HelD-RNAP complex, but we were not able to visualize any 183 NTP-bound state by cryo-EM. ...
Context 4
... reconstituted a complex of Msm RNAP core and Msm HelD from purified 78 recombinant proteins ( Figure S2), and froze an isolated homogenous fraction of the complex 79 on cryo-EM grids. We collected multiple preliminary cryo-EM datasets, which allowed us to 80 optimize the cryo-EM conditions for high-resolution three-dimensional (3D) single-particle the RNAP core. ...
Context 5
... 1A-2A heterodimer establishes the canonical tertiary structure to form an NTP-176 binding pocket. Conserved residues of motifs Q, I, II, ~III, IIIa, Va, and VI are then likely involved 177 in ATP binding 7,18 (Figure 2d) while motifs and residues typical for DNA binding are missing. ...
Context 6
... /2020 towards a pyrimidine-containing counterpart (Figure 2e, S7f). We also added ATP or non-182 hydrolysable ATP analogue to the HelD-RNAP complex, but we were not able to visualize any 183 NTP-bound state by cryo-EM. ...