https://ogma.newcastle.edu.au/vital/access/ /manager/Index ${session.getAttribute("locale")} 5 https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:20794 Firmicutes phylum of Gram-positive bacteria and have named it ε. Previously ε had been identified as a small protein (ω₁) that copurified with RNA polymerase. We have solved the structure of ε by X-ray crystallography and show that it is not an ω subunit. Rather, ε bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of ε shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of ε within the assembly of RNA polymerase core by single-particle analysis suggests that it binds toward the downstream side of the DNA binding cleft. Due to the structural similarity of ε with Gp2 and the fact they bind similar regions of RNA polymerase, we hypothesize that ε may serve a role in protection from phage infection.]]> Wed 11 Apr 2018 09:30:37 AEST ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:20277 Sat 24 Mar 2018 07:59:53 AEDT ]]> https://ogma.newcastle.edu.au/vital/access/ /manager/Repository/uon:4738 Sat 24 Mar 2018 07:21:09 AEDT ]]>