Open AccessPressure‐induced dissociation of ribosomes and elongation cycle intermediates
Author(s) -
GROSS Michael,
LEHLE Karla,
JAENICKE Rainer,
NIERHAUS Knud H.
Publication year - 1993
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1993.tb18397.x
Subject(s) - ribosome , elongation , biosynthesis , hydrostatic pressure , dissociation (chemistry) , protein biosynthesis , chemistry , biophysics , biochemistry , elongation factor , limiting , in vivo , microbiology and biotechnology , stereochemistry , enzyme , biology , rna , materials science , organic chemistry , thermodynamics , genetics , physics , gene , metallurgy , ultimate tensile strength , mechanical engineering , engineering
Pressure‐induced dissociation of ribosomes has been considered a major reason for the inhibition of protein biosynthesis and, hence, bacterial growth at high hydrostatic pressure [Jaenicke, R. (1981) Annu. Rev. Biophys. Bioeng. 10 , 1–67]. We reexamined the issue, using a buffer system with polyamines that has been optimized to reproduce in‐vivo ‐like performance of protein biosynthesis in vitro . By slightly modifying this buffer, we were able to find conditions that stabilize functional ribosomal complexes against the dissociating effect of pressure up to 100 MPa and uncharged tight couples up to 60 MPa. Approaching the physiological conditions by reducing the Mg 2+ concentration down to 4 mM, one finds a significant destabilization of the post‐translocational complex, which represents the most pressure‐sensitive intermediate of the elongation cycle and is possibly the limiting factor for the pressure‐induced block of protein biosynthesis and bacterial growth.