Peptidyl puromycin synthesis; effect of several antibiotics which act on 50 S ribosomal subunits
نویسندگان
چکیده
منابع مشابه
Studies on transfer ribonucleic acid-ribosome complexes. XXI. Effect of antibiotics on peptidyl-puromycin synthesis by mammalian polyribosomes.
The effect of antibiotics and other agents on-peptide bond synthesis by mammalian polyribosomes was determined by studying peptidyl-puromycin synthesis. Sparsomycin, anisomycin, cycloheximide, gougerotin, blasticidin S, and cryptopleurine inhibited the reaction. Sparsomycin and anisomytin inhibited the peptidyl-puromycin synthesis competitively with respect to puromycin. Arabinose analogs of pu...
متن کاملPeptidyl-puromycin synthesis on polyribosomes from Escherichia coli.
Peptide bond synthesis was studied with native polyribosomes of E. coli. With the use of this system for transpeptidation, it was possible to show that a single K(+) activates the ribosome monomers of polyribosomes; that protonation of a single group (probably imidazole or an N-terminal amino group) with a pK(a) equal to about 7.2 inactivates the transpeptidase complex; that Mn(++) can substitu...
متن کاملRibosomal protein L27 participates in both 50 S subunit assembly and the peptidyl transferase reaction.
Protein L27 has been implicated as a constituent of the peptidyl transferase center of the Escherichia coli 50 S ribosomal subunit by a variety of experimental observations. To define better the functional role of this protein, we constructed a strain in which the rpmA gene, which encodes L27, was replaced by a kanamycin resistance marker. The deletion mutant grows five to six times slower than...
متن کاملToxic effect of puromycin on erythrocyte membranes which is unrelated to inhibition of protein synthesis.
Exposure of rabbit or human erythrocytes to concentrations of puromycin as low as 7 x 10(-4)M for 2 hr causes damage to the cell membrane, as evidenced by increased susceptibility of the cells to hyposmotic lysis, increased cell rigidity, and ultrastructural changes consistent with severe membrane damage. Puromycin causes a concentration-dependent internalization of the erythrocyte membrane, re...
متن کاملThe oxazolidinone antibiotics perturb the ribosomal peptidyl-transferase center and effect tRNA positioning.
The oxazolidinones represent the first new class of antibiotics to enter into clinical usage within the past 30 years, but their binding site and mechanism of action has not been fully characterized. We have determined the crystal structure of the oxazolidinone linezolid bound to the Deinococcus radiodurans 50S ribosomal subunit. Linezolid binds in the A site pocket at the peptidyltransferase c...
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ژورنال
عنوان ژورنال: FEBS Letters
سال: 1971
ISSN: 0014-5793
DOI: 10.1016/0014-5793(71)80666-x