Conformational changes in bacterial polysomes induced by amino acid starvation.
The effects of amino acid starvation on polysome conformation were analyzed comparatively in stringent (relA+) and relaxed (relA) bacteria by measuring the accessibility in vitro of ribosomal proteins to reductive methylation. In polysomes of stringent cells, the conformational state of two proteins (L13 and L29) appeared significantly changed by starvation. In polysomes isolated from relaxed mutants, the accessibility of five proteins (L5, L13, L29, L31 and L32) was found modified.
D000596:Amino Acids / Q000494:pharmacology*; D001426:Bacterial Proteins / Q000378:metabolism; D004926:Escherichia coli / Q000187:drug effects / Q000378:metabolism*; D011132:Polyribosomes / Q000187:drug effects / Q000378:metabolism*; D011487:Protein Conformation / Q000187:drug effects; D012269:Ribosomal Proteins / Q000378:metabolism
D000596:Amino Acids; D001426:Bacterial Proteins; D012269:Ribosomal Proteins