Structural highlights
FunctionRPOY_GEOS3 A non-essential component of RNA polymerase (RNAP) (Probable). Has a similar structure to bacteriophage T7 protein Gp2 (AC P03704), which is known to bind to RNAP in the DNA binding-cleft. Unlike Gp2 however, this protein does not inhibit transcription inititation (PubMed:25092033).[1] Publication Abstract from PubMedRNA polymerase in bacteria is a multisubunit protein complex that is essential for gene expression. We have identified a new subunit of RNA polymerase present in the high A+T firmicutes phylum of Gram positive bacteria, and have named it . Previously had been identified as a small protein (omega1) that co-purified with RNA polymerase. We have solved the structure of by X-ray crystallography and show that it is not an omega subunit. Rather, bears remarkable similarity to the Gp2 family of phage proteins involved in the inhibition of host cell transcription following infection. Deletion of shows no phenotype and has no effect on the transcriptional profile of the cell. Determination of the location of within the assembly of RNA polymerase core by single particle analysis suggests it binds towards the downstream side of the DNA binding cleft. Due to the structural similarity of with Gp2, and the fact they bind similar regions of RNA polymerase, we hypothesise that may serve a role in protection from phage infection.
From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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This page was last modified 08:30, 11 January 2023.