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Gene Review

PRT1  -  E3 ubiquitin-protein ligase PRT1

Arabidopsis thaliana

Synonyms: proteolysis 1
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Disease relevance of PRT1


High impact information on PRT1


Biological context of PRT1


Anatomical context of PRT1

  • Ubiquitin-dependent proteolysis is a major proteolytic pathway in the cytoplasm and nucleus of eukaryotic cells [9].
  • We identified 83 out of 100 known proteins of the thylakoid localized photosynthetic apparatus, including several new paralogues and some 20 proteins involved in protein insertion, assembly, folding, or proteolysis [13].
  • Seed-type vacuolar processing enzyme (VPE) activity is predicted to be essential for post-translational proteolysis of seed storage proteins in the protein storage vacuole of developing seeds [14].
  • Here we have investigated the proteolysis of the presequences that have been cleaved off inside mitochondria [15].
  • This suggests that regulation of plastid proteolysis by the Clp machinery is not through differential regulation of ClpP/R/S gene expression, but rather through substrate recognition mechanisms and regulated interaction of chaperone-like molecules (ClpS1,2 and others) to the ClpP/R core [16].

Associations of PRT1 with chemical compounds

  • The thylakoid membrane of clpr2-1 showed increased carotenoid content, partial inactivation of photosystem II, and upregulated thylakoid proteases and stromal chaperones, suggesting an imbalance in chloroplast protein homeostasis and a well-coordinated network of proteolysis and chaperone activities [17].
  • In addition, we identified novel ABA-responsive gene families including those encoding ribosomal proteins and proteins involved in regulated proteolysis [18].
  • The cell biology of the COP/DET/FUS proteins. Regulating proteolysis in photomorphogenesis and beyond [19]?
  • The proteins that changed in quantity during the first day of cold acclimation include those that are associated with membrane repair by membrane fusion, protection of the membrane against osmotic stress, enhancement of CO2 fixation, and proteolysis [20].

Physical interactions of PRT1

  • Arabidopsis ERD1 is a ClpC-like protein that sequence analysis suggests may interact with the chloroplast-localized ClpP protease to facilitate proteolysis [21].
  • Expressed and purified AtSNAP33 also bound directly to the cytosolic domain of NtSyr1 and was sensitive to proteolysis by these toxins, suggesting that NtSyr1, a tobacco homologue of AtSNAP33, and coordinate SNAREs are likely to associate as partners for function in vivo [22].

Regulatory relationships of PRT1

  • The DELLA family members AtRGA or (Repressor of ga1-3) and OsSLR1 (SLENDER RICE1) proteins both appear to be subject to GA-induced proteolysis [23].
  • Also, we demonstrate that one of the mechanisms underlying GI protein oscillation occurs post-translationally via dark-induced proteolysis by the 26S proteasome [24].

Other interactions of PRT1

  • In Arabidopsis thaliana, GA derepresses its signaling pathway by inducing proteolysis of the DELLA protein REPRESSOR OF ga1-3 (RGA) [25].
  • In this work, the Arabidopsis thaliana INT6/eIF3e (AtINT6) protein was dissected using limited proteolysis, and a protease-resistant fragment containing the PCI domain was identified [26].
  • This proteolysis is proteasome dependent, implicating ZTL itself as substrate for ubiquitination [27].
  • A 60-kDa form of Atpk1 derived from the insect cell-expressed p70 was more highly phosphorylated than p70 in in vitro kinase assays, suggesting a negative regulatory domain can be removed by proteolysis [28].
  • Acceleration of Aux/IAA proteolysis is specific for auxin and independent of AXR1 [29].

Analytical, diagnostic and therapeutic context of PRT1


  1. Allelic characterization of the leaf-variegated mutation var2 identifies the conserved amino acid residues of FtsH that are important for ATP hydrolysis and proteolysis. Sakamoto, W., Miura, E., Kaji, Y., Okuno, T., Nishizono, M., Ogura, T. Plant Mol. Biol. (2004) [Pubmed]
  2. The gene complement for proteolysis in the cyanobacterium Synechocystis sp. PCC 6803 and Arabidopsis thaliana chloroplasts. Sokolenko, A., Pojidaeva, E., Zinchenko, V., Panichkin, V., Glaser, V.M., Herrmann, R.G., Shestakov, S.V. Curr. Genet. (2002) [Pubmed]
  3. Isolation and partial amino acid sequence of domains of nitrate reductase from spinach. Fido, R.J. Phytochemistry (1991) [Pubmed]
  4. Plant responses to ethylene gas are mediated by SCF(EBF1/EBF2)-dependent proteolysis of EIN3 transcription factor. Guo, H., Ecker, J.R. Cell (2003) [Pubmed]
  5. SINAT5 promotes ubiquitin-related degradation of NAC1 to attenuate auxin signals. Xie, Q., Guo, H.S., Dallman, G., Fang, S., Weissman, A.M., Chua, N.H. Nature (2002) [Pubmed]
  6. Identification of an SCF ubiquitin-ligase complex required for auxin response in Arabidopsis thaliana. Gray, W.M., del Pozo, J.C., Walker, L., Hobbie, L., Risseeuw, E., Banks, T., Crosby, W.L., Yang, M., Ma, H., Estelle, M. Genes Dev. (1999) [Pubmed]
  7. Intracellular trafficking and proteolysis of the Arabidopsis auxin-efflux facilitator PIN2 are involved in root gravitropism. Abas, L., Benjamins, R., Malenica, N., Paciorek, T., Wiśniewska, J., Wirniewska, J., Moulinier-Anzola, J.C., Sieberer, T., Friml, J., Luschnig, C. Nat. Cell Biol. (2006) [Pubmed]
  8. The Balance between Cell Division and Endoreplication Depends on E2FC-DPB, Transcription Factors Regulated by the Ubiquitin-SCFSKP2A Pathway in Arabidopsis. Del Pozo, J.C., Diaz-Trivino, S., Cisneros, N., Gutierrez, C. Plant Cell (2006) [Pubmed]
  9. Use of a reporter transgene to generate arabidopsis mutants in ubiquitin-dependent protein degradation. Bachmair, A., Becker, F., Schell, J. Proc. Natl. Acad. Sci. U.S.A. (1993) [Pubmed]
  10. Arabidopsis E2Fc functions in cell division and is degraded by the ubiquitin-SCF(AtSKP2) pathway in response to light. del Pozo, J.C., Boniotti, M.B., Gutierrez, C. Plant Cell (2002) [Pubmed]
  11. Regulation of phosphate homeostasis by MicroRNA in Arabidopsis. Chiou, T.J., Aung, K., Lin, S.I., Wu, C.C., Chiang, S.F., Su, C.L. Plant Cell (2006) [Pubmed]
  12. ORE9, an F-box protein that regulates leaf senescence in Arabidopsis. Woo, H.R., Chung, K.M., Park, J.H., Oh, S.A., Ahn, T., Hong, S.H., Jang, S.K., Nam, H.G. Plant Cell (2001) [Pubmed]
  13. In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Friso, G., Giacomelli, L., Ytterberg, A.J., Peltier, J.B., Rudella, A., Sun, Q., Wijk, K.J. Plant Cell (2004) [Pubmed]
  14. Redundant proteolytic mechanisms process seed storage proteins in the absence of seed-type members of the vacuolar processing enzyme family of cysteine proteases. Gruis, D.F., Selinger, D.A., Curran, J.M., Jung, R. Plant Cell (2002) [Pubmed]
  15. Isolation and identification of a novel mitochondrial metalloprotease (PreP) that degrades targeting presequences in plants. Stahl, A., Moberg, P., Ytterberg, J., Panfilov, O., Brockenhuus Von Lowenhielm, H., Nilsson, F., Glaser, E. J. Biol. Chem. (2002) [Pubmed]
  16. Clp protease complexes from photosynthetic and non-photosynthetic plastids and mitochondria of plants, their predicted three-dimensional structures, and functional implications. Peltier, J.B., Ripoll, D.R., Friso, G., Rudella, A., Cai, Y., Ytterberg, J., Giacomelli, L., Pillardy, J., van Wijk, K.J. J. Biol. Chem. (2004) [Pubmed]
  17. Downregulation of ClpR2 leads to reduced accumulation of the ClpPRS protease complex and defects in chloroplast biogenesis in Arabidopsis. Rudella, A., Friso, G., Alonso, J.M., Ecker, J.R., van Wijk, K.J. Plant Cell (2006) [Pubmed]
  18. Genome-wide gene expression profiling in Arabidopsis thaliana reveals new targets of abscisic acid and largely impaired gene regulation in the abi1-1 mutant. Hoth, S., Morgante, M., Sanchez, J.P., Hanafey, M.K., Tingey, S.V., Chua, N.H. J. Cell. Sci. (2002) [Pubmed]
  19. The cell biology of the COP/DET/FUS proteins. Regulating proteolysis in photomorphogenesis and beyond? Hardtke, C.S., Deng, X.W. Plant Physiol. (2000) [Pubmed]
  20. Mass spectrometric approach for identifying putative plasma membrane proteins of Arabidopsis leaves associated with cold acclimation. Kawamura, Y., Uemura, M. Plant J. (2003) [Pubmed]
  21. Chloroplast-targeted ERD1 protein declines but its mRNA increases during senescence in Arabidopsis. Weaver, L.M., Froehlich, J.E., Amasino, R.M. Plant Physiol. (1999) [Pubmed]
  22. Protein-binding partners of the tobacco syntaxin NtSyr1. Kargul, J., Gansel, X., Tyrrell, M., Sticher, L., Blatt, M.R. FEBS Lett. (2001) [Pubmed]
  23. A role for the ubiquitin-26S-proteasome pathway in gibberellin signaling. Itoh, H., Matsuoka, M., Steber, C.M. Trends Plant Sci. (2003) [Pubmed]
  24. Arabidopsis GIGANTEA protein is post-transcriptionally regulated by light and dark. David, K.M., Armbruster, U., Tama, N., Putterill, J. FEBS Lett. (2006) [Pubmed]
  25. The Arabidopsis F-box protein SLEEPY1 targets gibberellin signaling repressors for gibberellin-induced degradation. Dill, A., Thomas, S.G., Hu, J., Steber, C.M., Sun, T.P. Plant Cell (2004) [Pubmed]
  26. Identification and characterization of a proteolysis-resistant fragment containing the PCI domain in the Arabidopsis thaliana INT6/eIF3e translation factor. Murai, M.J., Carneiro, F.R., Gozzo, F.C., Ierardi, D.F., Pertinhez, T.A., Zanchin, N.I. Cell Biochem. Biophys. (2006) [Pubmed]
  27. Circadian phase-specific degradation of the F-box protein ZTL is mediated by the proteasome. Kim, W.Y., Geng, R., Somers, D.E. Proc. Natl. Acad. Sci. U.S.A. (2003) [Pubmed]
  28. atpk1, a novel ribosomal protein kinase gene from Arabidopsis. II. Functional and biochemical analysis of the encoded protein. Zhang, S.H., Broome, M.A., Lawton, M.A., Hunter, T., Lamb, C.J. J. Biol. Chem. (1994) [Pubmed]
  29. Acceleration of Aux/IAA proteolysis is specific for auxin and independent of AXR1. Zenser, N., Dreher, K.A., Edwards, S.R., Callis, J. Plant J. (2003) [Pubmed]
  30. The chaperone-like activity of a small heat shock protein is lost after sulfoxidation of conserved methionines in a surface-exposed amphipathic alpha-helix. Härndahl, U., Kokke, B.P., Gustavsson, N., Linse, S., Berggren, K., Tjerneld, F., Boelens, W.C., Sundby, C. Biochim. Biophys. Acta (2001) [Pubmed]
  31. Immunological detection of NADH-specific enoyl-ACP reductase from rape seed (Brassica napus)--induction, relationship of alpha and beta polypeptides, mRNA translation and interaction with ACP. Slabas, A.R., Cottingham, I.R., Austin, A., Hellyer, A., Safford, R., Smith, C.G. Biochim. Biophys. Acta (1990) [Pubmed]
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