Kumar Veerendra, Chen Yun, Ero Rya, Ahmed Tofayel, Tan Jackie, Li Zhe, Wong Andrew See Weng, Bhushan Shashi, Gao Yong-Gui
Institute of Molecular and Cell Biology, A*STAR, 138673, Singapore; School of Biological Sciences, Nanyang Technological University, 637551, Singapore.
School of Biological Sciences, Nanyang Technological University, 637551, Singapore.
Proc Natl Acad Sci U S A. 2015 Sep 1;112(35):10944-9. doi: 10.1073/pnas.1513216112. Epub 2015 Aug 17.
BPI-inducible protein A (BipA) is a member of the family of ribosome-dependent translational GTPase (trGTPase) factors along with elongation factors G and 4 (EF-G and EF4). Despite being highly conserved in bacteria and playing a critical role in coordinating cellular responses to environmental changes, its structures (isolated and ribosome bound) remain elusive. Here, we present the crystal structures of apo form and GTP analog, GDP, and guanosine-3',5'-bisdiphosphate (ppGpp)-bound BipA. In addition to having a distinctive domain arrangement, the C-terminal domain of BipA has a unique fold. Furthermore, we report the cryo-electron microscopy structure of BipA bound to the ribosome in its active GTP form and elucidate the unique structural attributes of BipA interactions with the ribosome and A-site tRNA in the light of its possible function in regulating translation.
BPI诱导蛋白A(BipA)是核糖体依赖性翻译GTP酶(trGTPase)家族的成员之一,与延伸因子G和4(EF-G和EF4)同属该家族。尽管它在细菌中高度保守,并在协调细胞对环境变化的反应中发挥关键作用,但其结构(分离状态和与核糖体结合状态)仍然未知。在此,我们展示了无apo形式以及结合了GTP类似物、GDP和鸟苷-3',5'-双二磷酸(ppGpp)的BipA的晶体结构。除了具有独特的结构域排列外,BipA的C端结构域具有独特的折叠方式。此外,我们报道了处于活性GTP形式的BipA与核糖体结合的冷冻电镜结构,并根据其在调节翻译中可能的功能,阐明了BipA与核糖体和A位点tRNA相互作用的独特结构特征。