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      Ubiquitin dependence of selective protein degradation demonstrated in the mammalian cell cycle mutant ts85.

      Cell
      Adenosine Triphosphate, metabolism, Animals, Cell Cycle, Cell Line, Chromosomal Proteins, Non-Histone, Female, Kinetics, Mammary Neoplasms, Experimental, physiopathology, Mice, Mutation, Neoplasm Proteins, isolation & purification, Nucleoproteins, Temperature, Ubiquitins

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          Abstract

          We have shown that covalent conjugation of ubiquitin to proteins is temperature-sensitive in the mouse cell cycle mutant ts85 due to a specifically thermolabile ubiquitin-activating enzyme (accompanying paper). We show here that degradation of short-lived proteins is also temperature sensitive in ts85 , in contrast to wild-type and revertant cells. While more than 70% of the prelabeled abnormal proteins (containing amino acid analogs) or puromycyl peptides are degraded within 4 hr at the permissive temperature in both ts85 and wild-type cells, less than 15% are degraded in ts85 cells at the nonpermissive temperature. Degradation of abnormal proteins and puromycyl peptides in both ts85 cells and wild-type cells is nonlysosomal and ATP-dependent. Immunochemical analysis shows a strong and specific reduction in the levels of in vivo labeled ubiquitin-protein conjugates at the nonpermissive temperature in ts85 cells. Degradation of normal, short-lived proteins is also specifically temperature sensitive in ts85 . We suggest that the contribution of ubiquitin-independent pathways to the degradation of short-lived proteins in this higher eucaryotic cell is no more than 10%, and possibly less.

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