D
IPR045135

26S proteasome regulatory subunit Rpn7, N-terminal

InterPro entry
Short nameRpn7_N

Description

This entry represents the N-terminal domain found in Rpn7 and Csn1.

The 26S proteasome plays a major role in ATP-dependent degradation of ubiquitinated proteins. Substrate specificity is conferred by the regulatory particle (RP), which can dissociate into stable lid and base subcomplexes. The regulatory subunit RPN7 is one of the lid subunits of the 26S proteasome and has been shown in Saccharomyces cerevisiae to be required for structural integrity
[2]
.

The COP9 signalosome is a conserved protein complex composed of eight subunits, where individual subunits of the complex have been linked to various signal transduction pathways leading to gene expression and cell cycle control
[3]
. The overall organisation and the amino acid sequences of the COP9 signalosome subunits resemble the lid subcomplex of the 19 S regulatory particle for the 26 S proteasome
[1]
. COP9 subunit 1 (CSN1 or GPS1) of the COP9 complex is an essential subunit of the complex with regard to both structural integrity and functionality. The N-terminal region of subunit 1 (CSN1-N) can inhibit c-fos expression from either a transfected template or a chromosomal transgene (fos-lacZ), and may contain the activity domain that confers most of the repression functions of CSN1. The C-terminal region of subunit 1 (CSN1-C) allows integration of the protein into the COP9 signalosome.

References

1.A subcomplex of the proteasome regulatory particle required for ubiquitin-conjugate degradation and related to the COP9-signalosome and eIF3. Glickman MH, Rubin DM, Coux O, Wefes I, Pfeifer G, Cjeka Z, Baumeister W, Fried VA, Finley D. Cell 94, 615-23, (1998). View articlePMID: 9741626

2.Rpn7 Is required for the structural integrity of the 26 S proteasome of Saccharomyces cerevisiae. Isono E, Saeki Y, Yokosawa H, Toh-e A. J. Biol. Chem. 279, 27168-76, (2004). View articlePMID: 15102831

3.The subunit 1 of the COP9 signalosome suppresses gene expression through its N-terminal domain and incorporates into the complex through the PCI domain. Tsuge T, Matsui M, Wei N. J. Mol. Biol. 305, 1-9, (2001). View articlePMID: 11114242

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