In the absence of ribosomal RNA synthesis, the ribosomal proteins of HeLa cells are synthesized normally and degraded rapidly.

摘要: Abstract It is possible to solubilize essentially the total protein complement from a lysate of HeLa cells. When such an extract displayed on two-dimensional polyacrylamide gel (pH 5·0 × sodium dodecyl sulfate) it isolate and identify 45 ribosomal proteins, five histones, numerous other proteins. Using this method we have measured directly synthesis proteins in presence actinomycin D. The results show that does not depend concurrent transcription precursor RNA. Furthermore, if RNA blocked for 25 hours by 10 ng actinomycin/ml, as well histone continues normally. This suggests either messenger exceedingly long-lived or mRNA can be uncoupled Ribosomal synthesized high low concentrations are unstable. They disappear, presumably through degradation, with half-lives 30 100 minutes, depending individual Under these conditions, histones several cell stable.