Poster Presentation The 44th Lorne Conference on Protein Structure and Function 2019

Molecular architecture of the E. faecalis anti-termination protein EutV bound to RNA (#252)

James L Walshe 1 , Karishma Patel 2 , Sandro F Ataide 2
  1. Victor Chang Cardiac Research Institute, Camperdown, NSW, Australia
  2. University of Sydney, Camperdown, NSW, Australia

Regulated transcription termination provides an efficient and responsive means to control gene expression.  Rho-independent termination occurs through the formation of a RNA stem-loop (T-loop) that disrupts the RNA polymerase elongation complex [1].  In anti-termination, a mutually exclusive RNA structure is formed, and in some cases stabilised by ANTAR domains of proteins, preventing termination [2].  We have determined the crystal structures of the stabilising anti-terminator protein EutV in its apo form, to 2.5 Å resolution, and bound to a double stem loop RNA, 3.8 Å resolution.  Our studies highlight the key interactions between conserved EutV residues and the RNA, as well as protein conformational changes undergone upon RNA binding.  Thus proposing a general model for ANTAR domain anti-termination

  1. Gusarov, I. and E. Nudler (1999). "The mechanism of intrinsic transcription termination." Molecular cell 3(4): 495-504.
  2. Ramesh, A., et al. (2012). "The mechanism for RNA recognition by ANTAR regulators of gene expression." PLoS Genet 8(6): e1002666-e1002666.