Rhodococcus Prokaryotic Ubiquitin-Like Protein (Pup) Is Degraded by Deaminase of Pup (Dop)

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Abstract

Prokaryotic ubiquitin-like protein (Pup) is a functional analog of ubiquitin. Post-translationally modified pupylated proteins are selectively degraded by a proteasome-dependent proteolytic system. Deaminase of Pup (Dop) activates Pup by deaminating the C-terminal from glutamine to glutamate, and subsequently activated Pup is conjugated to target proteins by proteasome accessory factor A. Dop is also involved in the removal of Pup from pupylated proteins. Deconjugated free Pup is capable of religating to target proteins. Although the pupylation system is well studied in <i>Mycobacterium</i>, little is known about it in other actinomycetes. Both <i>Rhodococcus</i> and <i>Mycobacterium</i> Dop remove Pup from pupylated proteins, but in these two bacteria, no accumulation of deconjugated free Pup from <i>Rhodococcus</i> is observed. Analysis of a model pupylated protein revealed that <i>Rhodococcus</i> Pup is degraded at multiple sites by Dop. The endopeptidase activity of Dop can be detected using a fluorogenic substrate in conjunction with aminopeptidase. Moreover, the enzymatic activity of the model enzyme increases when Pup is deconjugated. These results suggest that depupylated <i>Rhodococcus</i> Pup is not recycled for religation with target proteins, and that Pup not only functions as a degradation signal, but also regulates the enzymatic activity of target proteins by conjugation and deconjugation to them.

Journal

  • Bioscience, Biotechnology, and Biochemistry

    Bioscience, Biotechnology, and Biochemistry 76(10), 1959-1966, 2012-10-23

    Japan Society for Bioscience, Biotechnology, and Agrochemistry

References:  34

Codes

  • NII Article ID (NAID)
    10031126487
  • NII NACSIS-CAT ID (NCID)
    AA10824164
  • Text Lang
    ENG
  • Article Type
    ART
  • ISSN
    09168451
  • NDL Article ID
    024035970
  • NDL Call No.
    Z53-G223
  • Data Source
    CJP  NDL  J-STAGE 
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