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. 2020 Jul 2;9(7):832. doi: 10.3390/plants9070832

Table 1.

Comparison between 26S proteasomes and Clp protease.

Issues/Characteristics 26S Proteasomes Clp Protease
  1. Location

Cytoplasm and nucleus Plastid and mitochondria
  • 2.

    Components

19S regulatory particle and 20S core particle Chaperone subunit and proteolytic subunit
  • 3.

    Regulatory particle or Chaperone

19S regulatory particle, hexameric ring Chaperone subunit, hexameric ring
  • 4.

    Proteolytic subunit

20S core particle, heptagonal barrel-shaped ring Proteolytic subunit, tetradecameric barrel-shaped ring
  • 5.

    Components of Regulatory particle (RP) or Chaperone

Regulatory particle consists of base and lid.
Base has six ATPase subunits (Rpt1-Rpt6) and two non-ATPase subunits (Rpn1 and Rpn2).
Lid contains eight non-ATPase subunits (RPN3, 5–9, 11, and 12)
ClpC1, ClpC2, and ClpD constitute the chaperone subunit (in Arabidopsis thaliana)
  • 6.

    Components of Proteolytic subunit

Four ring. Inner two rings are β catalytic rings (β1-7) and outer two rings are α rings (α1-7) ClpP1, ClpP3, ClpP4, ClpP5, and ClpP6 constitute the proteolytic subunit (in Arabidopsis thaliana)
  • 7.

    Linker or adapters

Rpn10 and Rpn13 serve as linker between lid and base ClpS1 and ClpF serve as adapter for ClpC (in Arabidopsis thaliana)