Poster Presentation The 43rd Lorne Conference on Protein Structure and Function 2018

Similarity and diversity of EF-G, EF4(LepA), and BipA in protein synthesis, and the LCIB in CO2-concentrating mechanism (#174)

Yong-Gui Gao 1
  1. Nanyang Technological University, Singapore, SINGAPORE

Understanding the detailed mechanism of ribosome function is important not only as a fundamental issue in life science, but also because of many clinically relevant antibiotics targeting the ribosome. Recently, structural determination of ribosome in various states involving divers translational factors has generated a wealth of information on how genetic codes are precisely translated into proteins by ribosome. In addition to EF-G functioning in translocation, there are two other EF-G paralogs EF-4 and BipA, that are highly conserved in bacteria. There three translational GTPase factors share structural similarity, but with diverse functions. I will present our recent results on structural study of these factors in the ribosome.


In many aquatic phytoplankton, such as the eukaryotic algae C. reinhardtii, the CO2-concentrating mechanisms (CCMs) have evolved as an adaptation to maintain optimal photosynthetic activity, under CO2-limiting conditions. The limiting CO2-inducible B protein (LCIB) in C. reinhardtii is an essential factor for the CCMs, and it also involves the “air-dier” phenotype which was discovered more than three decades ago. In the second part, I will introduce our recent progress on structural and biochemical characterization of the LCIB proteins from divers microorganisms.