Premium
During amino acid starvation, RelA associates with ribosomes with an uncharged tRNA at the A site and synthesizes (p)ppGpp. Single‐molecule localization and tracking studies support a model in which RelA is active while bound to the ribosome. Shown is a gallery of 15‐step, 150 ms long experimental trajectories (artifi cially colored) of RelA‐YFP in E. coli cells starved of amino acids. The trace in the upper right corner has an overall height of approximately 2 μm. For details, see the article by Li et al. on pp. 571–585 of this issue.
Publication year - 2016
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/mmi.13177
Subject(s) - ribosome , transfer rna , biology , amino acid , computational biology , biochemistry , gene , rna