Abstract
An electrophoretically distinct ribosomal protein fraction derived from the large (60 S) subunit of rabbit reticulocyte ribosomes appears to contain the sulfhydryl group(s), the integrity of which is required for the poly (U)-directed binding of phenylalanyl-transfer RNA. Since the addition of the translocase enzyme (T-2) is required to confer puromycin reactivity on these molecules, it is therefore assumed that they are in the acceptor site. This contrasts with studies in prokaryotic systems, which indicate that both N-ethyl maleimide sensitivity and the acceptor site are associated with the small ribosomal subunit. It is similar to that system, however, in that the proteins implicated have multiple sulfhydryl groups, and probably only one of these is required for phenylalanyl-transfer RNA binding activity.
Published Version
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