Chandra Sekhar Mandava

TL;DR: Heteronuclear NMR spectroscopy is demonstrated that L12 binds directly to the factors IF2,EF-Tu, EF-G, and RF3 from Escherichia coli, and the region of L12 involved in these interactions is mapped, indicating that the L12-factor complexes will be highly populated on the ribosome, because of the high local concentration of ribosomes-bound factor with respect to L12.

TL;DR: Kinetics and cryo-electronmicroscopy data provide insights into GTPase ObgE's role as a ribosome anti-association factor that is modulated by nutrient availability, coupling growth control to ribosomes biosynthesis and protein translation.

TL;DR: Fast kinetics and cryo-EM data reveal that HflX is a heat shock–induced ribosome-splitting factor capable of dissociating vacant as well as mRNA-associated ribosomes with deacylated tRNA in the peptidyl site, and suggest a primary role of HFlX in rescuing translationally arrested ribosom under stress conditions.

TL;DR: A new strain of Escherichia coli (JE28) is designed by an in-frame fusion of a nucleotide sequence encoding a hexa-histidine affinity tag at the 3′-end of the single copy rplL gene (encoding the ribosomal protein L12) at the chromosomal site of the wild-type strain MG1655.

TL;DR: In vitro analysis by fast kinetics revealed that single L12 dimer ribosomes from JE105 are defective in two major steps of translation, namely initiation and elongation involving translational GTPases IF2 and EF-G.