메뉴 건너뛰기




Volumn 13, Issue 7, 2014, Pages 3223-3230

Proteomic analysis of the 26S proteasome reveals its direct interaction with transit peptides of plastid protein precursors for their degradation

Author keywords

26S proteasome; Arabidopsis thaliana; proteomic analysis; transit peptide; yeast two hybrid assay

Indexed keywords

BENZYLOXYCARBONYLLEUCYLLEUCYLLEUCINAL; CHLOROPLAST PROTEIN; GLYCEROL; PROTEASOME; PROTEIN PRECURSOR; ARABIDOPSIS PROTEIN; ATP DEPENDENT 26S PROTEASE; PEPTIDE FRAGMENT;

EID: 84903734722     PISSN: 15353893     EISSN: 15353907     Source Type: Journal    
DOI: 10.1021/pr401245g     Document Type: Article
Times cited : (23)

References (41)
  • 1
    • 67349254570 scopus 로고    scopus 로고
    • The ubiquitin-26S proteasome system at the nexus of plant biology
    • Vierstra, R. D. The ubiquitin-26S proteasome system at the nexus of plant biology Nat. Rev. Mol. Cell Biol. 2009, 10, 385-397
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 385-397
    • Vierstra, R.D.1
  • 3
    • 0029042511 scopus 로고
    • Crystal structure of the 20S proteasome from the archaeon T acidophilum at 3.4 Å resolution
    • Lowe, J.; Stock, D.; Jap, B.; Zwickl, P.; Baumeister, W.; Huber, R. Crystal structure of the 20S proteasome from the archaeon T. acidophilum at 3.4 Å resolution Science 1995, 268, 533-539
    • (1995) Science , vol.268 , pp. 533-539
    • Lowe, J.1    Stock, D.2    Jap, B.3    Zwickl, P.4    Baumeister, W.5    Huber, R.6
  • 4
    • 1542344435 scopus 로고    scopus 로고
    • Proteasomes and their kin: Proteases in the machine age
    • Pickart, C. M.; Cohen, R. E. Proteasomes and their kin: proteases in the machine age Nat. Rev. Mol. Cell Biol. 2004, 5, 177-187
    • (2004) Nat. Rev. Mol. Cell Biol. , vol.5 , pp. 177-187
    • Pickart, C.M.1    Cohen, R.E.2
  • 5
    • 34548274872 scopus 로고    scopus 로고
    • Docking of the proteasomal ATPases carboxyl termini in the 20S proteasomes alpha ring opens the gate for substrate entry
    • Smith, D. M.; Chang, S. C.; Park, S.; Finley, D.; Cheng, Y.; Goldberg, A. L. Docking of the proteasomal ATPases carboxyl termini in the 20S proteasomes alpha ring opens the gate for substrate entry Mol. Cell 2007, 27, 731-744
    • (2007) Mol. Cell , vol.27 , pp. 731-744
    • Smith, D.M.1    Chang, S.C.2    Park, S.3    Finley, D.4    Cheng, Y.5    Goldberg, A.L.6
  • 6
    • 33749348820 scopus 로고    scopus 로고
    • A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes
    • Hamazaki, J.; Iemura, S.; Natsume, T.; Yashiroda, H.; Tanaka, K.; Murata, S. A novel proteasome interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes EMBO J. 2006, 25, 4524-4536
    • (2006) EMBO J. , vol.25 , pp. 4524-4536
    • Hamazaki, J.1    Iemura, S.2    Natsume, T.3    Yashiroda, H.4    Tanaka, K.5    Murata, S.6
  • 7
    • 65849101541 scopus 로고    scopus 로고
    • Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle
    • Saeki, Y.; Toh-E, A.; Kudo, T.; Kawamura, H.; Tanaka, K. Multiple proteasome-interacting proteins assist the assembly of the yeast 19S regulatory particle Cell 2009, 137, 900-913
    • (2009) Cell , vol.137 , pp. 900-913
    • Saeki, Y.1    Toh-E, A.2    Kudo, T.3    Kawamura, H.4    Tanaka, K.5
  • 8
    • 77955485244 scopus 로고    scopus 로고
    • Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes
    • Book, A. J.; Gladman, N. P.; Lee, S.-S.; Scalf, M.; Smith, L. M.; Vierstra, R. D. Affinity purification of the Arabidopsis 26 S proteasome reveals a diverse array of plant proteolytic complexes J. Biol. Chem. 2010, 285, 25554-25569
    • (2010) J. Biol. Chem. , vol.285 , pp. 25554-25569
    • Book, A.J.1    Gladman, N.P.2    Lee, S.-S.3    Scalf, M.4    Smith, L.M.5    Vierstra, R.D.6
  • 9
    • 0037390990 scopus 로고    scopus 로고
    • The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling
    • Smallea, J.; Kurepaa, J.; Yanga, P.; Emborga, T. J.; Babiychukb, E.; Kushnirb, S.; Vierstra, R. D. The pleiotropic role of the 26S proteasome subunit RPN10 in Arabidopsis growth and development supports a substrate-specific function in abscisic acid signaling Plant Cell 2003, 15, 965-980
    • (2003) Plant Cell , vol.15 , pp. 965-980
    • Smallea, J.1    Kurepaa, J.2    Yanga, P.3    Emborga, T.J.4    Babiychukb, E.5    Kushnirb, S.6    Vierstra, R.D.7
  • 14
    • 20444438444 scopus 로고    scopus 로고
    • Regulation of secondary cell wall development by cortical microtubules during tracheary element differentiation in Arabidopsis cell suspensions
    • Oda, Y.; Mimura, T.; Hasezawa, S. Regulation of secondary cell wall development by cortical microtubules during tracheary element differentiation in Arabidopsis cell suspensions Plant Physiol. 2005, 137, 1027-1036
    • (2005) Plant Physiol. , vol.137 , pp. 1027-1036
    • Oda, Y.1    Mimura, T.2    Hasezawa, S.3
  • 15
    • 80053563165 scopus 로고    scopus 로고
    • Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis
    • Sato, T.; Maekawa, S.; Yasuda, S.; Domeki, Y.; Sueyoshi, K.; Fujiwara, M.; Fukao, Y.; Goto, D. B.; Yamaguchi, J. Identification of 14-3-3 proteins as a target of ATL31 ubiquitin ligase, a regulator of the C/N response in Arabidopsis Plant J. 2011, 68, 137-146
    • (2011) Plant J. , vol.68 , pp. 137-146
    • Sato, T.1    Maekawa, S.2    Yasuda, S.3    Domeki, Y.4    Sueyoshi, K.5    Fujiwara, M.6    Fukao, Y.7    Goto, D.B.8    Yamaguchi, J.9
  • 16
    • 33646854930 scopus 로고    scopus 로고
    • Proteomics of Rac GTPase signaling reveals its predominant role in elicitor-induced defense response of cultured rice cells
    • Fujiwara, M.; Umemura, K.; Kawasaki, T.; Shimamoto, K. Proteomics of Rac GTPase signaling reveals its predominant role in elicitor-induced defense response of cultured rice cells Plant Physiol. 2006, 140, 734-745
    • (2006) Plant Physiol. , vol.140 , pp. 734-745
    • Fujiwara, M.1    Umemura, K.2    Kawasaki, T.3    Shimamoto, K.4
  • 18
    • 72649086621 scopus 로고    scopus 로고
    • Identification of zinc-responsive proteins in the roots of Arabidopsis thaliana using a highly improved method of two-dimensional electrophoresis
    • Fukao, Y.; Ferjani, A.; Fujiwara, M.; Nishimori, Y.; Ohtsu, I. Identification of zinc-responsive proteins in the roots of Arabidopsis thaliana using a highly improved method of two-dimensional electrophoresis Plant Cell Physiol. 2009, 50, 2234-2239
    • (2009) Plant Cell Physiol. , vol.50 , pp. 2234-2239
    • Fukao, Y.1    Ferjani, A.2    Fujiwara, M.3    Nishimori, Y.4    Ohtsu, I.5
  • 19
    • 77956467961 scopus 로고    scopus 로고
    • Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants
    • Igawa, T.; Fujiwara, M.; Tanaka, I.; Fukao, Y.; Yanagawa, Y. Characterization of bacterial-type phosphoenolpyruvate carboxylase expressed in male gametophyte of higher plants BMC Plant Biol. 2010, 10, 200
    • (2010) BMC Plant Biol. , vol.10 , pp. 200
    • Igawa, T.1    Fujiwara, M.2    Tanaka, I.3    Fukao, Y.4    Yanagawa, Y.5
  • 22
    • 0036500015 scopus 로고    scopus 로고
    • Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis
    • Suzuki, G.; Yanagawa, Y.; Kwok, S. F.; Matsui, M.; Deng, X. W. Arabidopsis COP10 is a ubiquitin-conjugating enzyme variant that acts together with COP1 and the COP9 signalosome in repressing photomorphogenesis Genes Dev. 2002, 16, 554-559
    • (2002) Genes Dev. , vol.16 , pp. 554-559
    • Suzuki, G.1    Yanagawa, Y.2    Kwok, S.F.3    Matsui, M.4    Deng, X.W.5
  • 24
    • 84879478354 scopus 로고    scopus 로고
    • Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis
    • Kim, D. Y.; Scalf, M.; Smith, L. M.; Vierstra, R. D. Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis Plant Cell 2013, 25, 1523-1540
    • (2013) Plant Cell , vol.25 , pp. 1523-1540
    • Kim, D.Y.1    Scalf, M.2    Smith, L.M.3    Vierstra, R.D.4
  • 25
    • 84879886539 scopus 로고    scopus 로고
    • Cytoplasmic proteasomes are not indispensable for cell growth in Saccharomyces cerevisiae
    • Tsuchiya, H.; Arai, N.; Tanaka, K.; Saeki, Y. Cytoplasmic proteasomes are not indispensable for cell growth in Saccharomyces cerevisiae Biochem. Biophys. Res. Commun. 2013, 436, 372-376
    • (2013) Biochem. Biophys. Res. Commun. , vol.436 , pp. 372-376
    • Tsuchiya, H.1    Arai, N.2    Tanaka, K.3    Saeki, Y.4
  • 26
    • 75649148551 scopus 로고    scopus 로고
    • Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis
    • Lee, S.; Lee, D. W.; Lee, Y.; Mayer, U.; Stierhof, Y.-D.; Lee, S.; Jürgens, G.; Hwang, I. Heat shock protein cognate 70-4 and an E3 ubiquitin ligase, CHIP, mediate plastid-destined precursor degradation through the ubiquitin-26S proteasome system in Arabidopsis Plant Cell 2009, 21, 3984-4001
    • (2009) Plant Cell , vol.21 , pp. 3984-4001
    • Lee, S.1    Lee, D.W.2    Lee, Y.3    Mayer, U.4    Stierhof, Y.-D.5    Lee, S.6    Jürgens, G.7    Hwang, I.8
  • 27
    • 33846041276 scopus 로고    scopus 로고
    • The chloroplast protease subunit ClpP4 is a substrate of the E3 ligase AtCHIP and plays an important role in chloroplast function
    • Shen, G.; Yan, J.; Pasapula, V.; Luo, J.; He, C.; Clarke, A. K.; Zhang, H. The chloroplast protease subunit ClpP4 is a substrate of the E3 ligase AtCHIP and plays an important role in chloroplast function Plant J. 2007, 49, 228-237
    • (2007) Plant J. , vol.49 , pp. 228-237
    • Shen, G.1    Yan, J.2    Pasapula, V.3    Luo, J.4    He, C.5    Clarke, A.K.6    Zhang, H.7
  • 28
    • 35148872652 scopus 로고    scopus 로고
    • The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts
    • Shen, G.; Adam, Z.; Zhang, H. The E3 ligase AtCHIP ubiquitylates FtsH1, a component of the chloroplast FtsH protease, and affects protein degradation in chloroplasts Plant J. 2007, 52, 309-321
    • (2007) Plant J. , vol.52 , pp. 309-321
    • Shen, G.1    Adam, Z.2    Zhang, H.3
  • 29
    • 1242291789 scopus 로고    scopus 로고
    • CHIP: A link between the chaperone and proteasome systems
    • McDonough, H.; Patterson, C. CHIP: a link between the chaperone and proteasome systems Cell Stress Chaperones 2003, 8, 303-308
    • (2003) Cell Stress Chaperones , vol.8 , pp. 303-308
    • McDonough, H.1    Patterson, C.2
  • 30
    • 27744432391 scopus 로고    scopus 로고
    • Plastids unleashed: Their development and their integration in plant development
    • Lopez-Juez, E.; Pyke, K. A. Plastids unleashed: their development and their integration in plant development Int. J. Dev. Biol. 2005, 49, 557-577
    • (2005) Int. J. Dev. Biol. , vol.49 , pp. 557-577
    • Lopez-Juez, E.1    Pyke, K.A.2
  • 31
    • 9644280977 scopus 로고    scopus 로고
    • Cooperation of molecular chaperones with the ubiquitin/proteasome system
    • Esser, C.; Alberti, S.; Höhfeld, J. Cooperation of molecular chaperones with the ubiquitin/proteasome system Biochim. Biophys. Acta 2004, 1695, 171-188
    • (2004) Biochim. Biophys. Acta , vol.1695 , pp. 171-188
    • Esser, C.1    Alberti, S.2    Höhfeld, J.3
  • 32
    • 0042320478 scopus 로고    scopus 로고
    • Ubiquitylation as a quality control system for intracellular proteins
    • Hatakeyama, S.; Nakayama, K. I. Ubiquitylation as a quality control system for intracellular proteins J. Biochem. 2003, 134, 1-8
    • (2003) J. Biochem. , vol.134 , pp. 1-8
    • Hatakeyama, S.1    Nakayama, K.I.2
  • 33
    • 84856658975 scopus 로고    scopus 로고
    • The phosphorylation state of chloroplast transit peptides regulates preprotein import
    • Lamberti, G.; Drurey, C.; Soll, J.; Schwenkert, S. The phosphorylation state of chloroplast transit peptides regulates preprotein import Plant Signaling Behav. 2011, 6, 1918-1920
    • (2011) Plant Signaling Behav. , vol.6 , pp. 1918-1920
    • Lamberti, G.1    Drurey, C.2    Soll, J.3    Schwenkert, S.4
  • 34
    • 70349780560 scopus 로고    scopus 로고
    • The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries
    • Sha, Z.; Brill, L. M.; Cabrera, R.; Kleifeld, O.; Scheliga, J. S.; Glickman, M. H.; Chang, E. C.; Wolf, D. a. The eIF3 interactome reveals the translasome, a supercomplex linking protein synthesis and degradation machineries Mol. Cell 2009, 36, 141-152
    • (2009) Mol. Cell , vol.36 , pp. 141-152
    • Sha, Z.1    Brill, L.M.2    Cabrera, R.3    Kleifeld, O.4    Scheliga, J.S.5    Glickman, M.H.6    Chang, E.C.7    De, A.W.8
  • 38
    • 0037129213 scopus 로고    scopus 로고
    • A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal
    • Lam, Y. A.; Lawson, T. G.; Velayutham, M.; Zweier, J. L.; Pickart, C. M. A proteasomal ATPase subunit recognizes the polyubiquitin degradation signal Nature 2002, 416, 763-767
    • (2002) Nature , vol.416 , pp. 763-767
    • Lam, Y.A.1    Lawson, T.G.2    Velayutham, M.3    Zweier, J.L.4    Pickart, C.M.5
  • 39
    • 4344559454 scopus 로고    scopus 로고
    • An unstructured initiation site is required for efficient proteasome-mediated degradation
    • Prakash, S.; Tian, L.; Ratliff, K. S.; Lehotzky, R. E.; Matouschek, A. An unstructured initiation site is required for efficient proteasome-mediated degradation Nat. Struct. Mol. Biol. 2004, 11, 830-837
    • (2004) Nat. Struct. Mol. Biol. , vol.11 , pp. 830-837
    • Prakash, S.1    Tian, L.2    Ratliff, K.S.3    Lehotzky, R.E.4    Matouschek, A.5
  • 41
    • 0034308219 scopus 로고    scopus 로고
    • Chloroplast transit peptides: Structure, function and evolution
    • Bruce, B. D. Chloroplast transit peptides: structure, function and evolution Trends Cell Biol. 2000, 10, 440-447
    • (2000) Trends Cell Biol. , vol.10 , pp. 440-447
    • Bruce, B.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.