Open AccessAlteration of Ribosomal Proteins and Functions by 2‐Methoxy‐5‐nitrotropone
Author(s) -
Ballesta Juan P. G.,
Montejo Vicente,
Hernandez Francisco,
Vazquez David
Publication year - 1974
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1111/j.1432-1033.1974.tb03326.x
Subject(s) - ribosome , ribosomal protein , protein biosynthesis , eukaryotic ribosome , peptidyl transferase , gtpase , thiostrepton , biochemistry , elongation factor , chemistry , polyacrylamide gel electrophoresis , ribosomal rna , chloramphenicol , gtp' , peptide , biology , enzyme , rna , antibiotics , gene
The effect of 2‐methoxy‐5‐nitrotropone on the ribosome has been studied. Treated particles are inactivated for polypeptide synthesis, aminoacyl‐tRNA binding, and elongation‐factor‐dependent GTPase but catalize peptide bond formation. Treated particles (either 70‐S ribosomes or ribosomal cores lacking proteins L7 and L12) recover their ability to hydrolyze GTP, but not to support polypeptide synthesis or aminoacyl‐tRNA binding, upon the addition of these two untreated proteins. However, even in the absence of the added proteins the treated particles are able to carry out substantial GTP hydrolysis in the presence of 20% methanol. Interaction of particles with antibiotics such as chloramphenicol and thiostrepton is not affected by treatment. When proteins from treated 50‐S subunits were analyzed by two‐dimensional polyacrylamide gel electrophoresis, only proteins L3, and L15 were found not to be affected by the treatment. Proteins L1, L2, L4, L10, L13, L16, L17, L18, L22 and L24 showed spots of much less intensity than the controls and the other protein spots were not detected. A comparison of the resistant proteins with those present on CsCl‐derived cores points to protein L15 as possibly involved in the peptidyl transferase centre of the ribosome.