*MTBC, Mycobacterium tuberculosis complex; PCR, polymerase chain reaction; AFB, acid-fast bacilli; n, no. of samples.
In the DNA-bound complex, the polymerase is tethered to the DNA through multiple contacts with the clamp.
Following NTP binding and conversion to the catalysis-competent ternary complex, the polymerase revealed an improved affinity for the template.
In the extended MST network (Fig. 4), the subdivision of the complex into polymerase complexes I, II and III is clearly visible which is not the case for the complete or connected networks.
During crystallization of the ternary complex, the polymerase extended the 3′-end of the RNA primer by addition of two deoxyguanosine nucleotides.
Liver and tracheobronchial lymph node specimens collected at necropsy were positive by AFB stain and positive for M. tuberculosis complex by polymerase chain reaction.
We show that, independently of thermodynamic stability of the elongation complex, RNA polymerase directly 'senses' the shape and/or identity of base pairs of the RNA DNA hybrid.
It is confirmed by the fact that the complex 'RNA polymerase II' transcribes genetic information into messages for ribosomes to produce proteins.
This study evaluated the use of HaloTag for capturing a large protein complex, RNA polymerase, using RpoA as the bait protein.
We used antibodies against RUNX1, the ETO moiety of RUNX1/ETO, LMO2 as a member of the RUNX1/ETO complex, RNA-Polymerase II, and acetylated histone H3 for ChIP.
This hybrid might destabilize the RNA polymerase-6S RNA complex, and rescue polymerase activity from the repressed status.
