Protein turnover in the extreme thermophile Thermus aquaticus.
AUTOR(ES)
Kenkel, T
RESUMO
Protein turnover in the extreme bacterial thermophile Thermus aquaticus was examined in exponential cultures at 75 degrees C. The relative amount of [3H]leucine incorporated into trichloroacetic acid-insoluble material was stable in pulse-chase experiments assayed over 2.5 h. The trichloroacetic acid-insoluble radioactive leucine was stable upon the addition of chloramphenicol, which blocks protein synthesis in T. aquaticus. The specific activity of a phosphate-repressible alkaline phosphatase, investigated in the presence of chloramphenicol, did not decrease. The addition of excess orthophosphate to cultures derepressed for the alkaline phosphatase did not show a marked effect on the specific activity over a 2-h period. On the basis of these four experiments, it does not appear that a high protein turnover rate is essential for the thermophily of T. aquaticus at 75 degrees C.
ACESSO AO ARTIGO
http://www.pubmedcentral.nih.gov/articlerender.fcgi?artid=216680Documentos Relacionados
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