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Inhibition of the elongation step of protein synthesis by vaccinia virus
Author(s) -
Tas P.W.L.,
Martini O.H.W.
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80657-7
Subject(s) - elongation , protein biosynthesis , anisomycin , vaccinia , ribosome , reticulocyte , elongation factor , translation (biology) , puromycin , chemistry , protein synthesis inhibitor , lysis , eukaryotic translation , cycloheximide , biology , biophysics , biochemistry , rna , messenger rna , recombinant dna , materials science , gene , metallurgy , ultimate tensile strength
Vaccinia cores inhibit translation in cell‐free protein synthesis systems at two stages: initiation; and, as shown here, elongation. The former effect tends to obscure the latter. Elongation control could, however, be revealed as follows: when, in a reticulocyte of L‐cell lysate, initiation was blocked by a drug (edein), the residual [ 35 S]methionine incorporation was severely reduced by the subsequent addition of vaccinia cores. The elongation block could also be demonstrated by analysis of ribosome profiles: treatment with edein alone permitted ribosomal run‐off; treatment with either the elongation inhibition anisomycin or with cores preserved the polyribosomes.