메뉴 건너뛰기




Volumn 444, Issue 4, 2014, Pages 575-580

Classification and interaction modes of 40 rice E2 ubiquitin-conjugating enzymes with 17 rice ARM-U-box E3 ubiquitin ligases

Author keywords

ARM U box E3 ubiquitin ligase; E2 ubiquitin conjugating enzyme; E2 E3 interaction; Rice (Oryza sativa L.); Ubiquitination

Indexed keywords

ARM-U-BOX E3 UBIQUITIN-LIGASE; E2 UBIQUITIN-CONJUGATING ENZYME; E2-E3 INTERACTION; RICE (ORYZA SATIVA L.); UBIQUITINATION;

EID: 84894537861     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2014.01.098     Document Type: Article
Times cited : (45)

References (37)
  • 1
    • 34250897234 scopus 로고    scopus 로고
    • Ubiquitin, hormones and biotic stress in plants
    • K. Dreher, and J. Callis Ubiquitin, hormones and biotic stress in plants Ann. Bot. (Lond.) 99 2007 787 822
    • (2007) Ann. Bot. (Lond.) , vol.99 , pp. 787-822
    • Dreher, K.1    Callis, J.2
  • 2
    • 67349254570 scopus 로고    scopus 로고
    • The ubiquitin-26S proteasome system at the nexus of plant biology
    • R.D. Vierstra The ubiquitin-26S proteasome system at the nexus of plant biology Nat. Rev. Mol. Cell Biol. 11 2009 385 397
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.11 , pp. 385-397
    • Vierstra, R.D.1
  • 3
    • 84872324586 scopus 로고    scopus 로고
    • Roles of various Cullin-RING E3 ligases in hormonal and stress responses in plats
    • K.-I. Seo, E. Song, S. Chung, and J.-H. Lee Roles of various Cullin-RING E3 ligases in hormonal and stress responses in plats J. Plant Biol. 55 2012 421 428
    • (2012) J. Plant Biol. , vol.55 , pp. 421-428
    • Seo, K.-I.1    Song, E.2    Chung, S.3    Lee, J.-H.4
  • 4
    • 67349256160 scopus 로고    scopus 로고
    • Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signaling pathways
    • B.A. Schulman, and J.W. Harper Ubiquitin-like protein activation by E1 enzymes: The apex for downstream signaling pathways Nat. Rev. Mol. Cell Biol. 10 2009 319 331
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 319-331
    • Schulman, B.A.1    Harper, J.W.2
  • 5
    • 70350461507 scopus 로고    scopus 로고
    • Building ubiquitin chains: E2 enzymes at work
    • Y. Ye, and M. Rape Building ubiquitin chains: E2 enzymes at work Nat. Rev. Mol. Cell Biol. 10 2009 755 764
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 755-764
    • Ye, Y.1    Rape, M.2
  • 6
    • 0032539909 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death
    • A. Ciechanover, and A.L. Schwartz The ubiquitin-proteasome pathway: The complexity and myriad functions of proteins death Proc. Natl. Acad. Sci. USA 95 1998 2727 2730
    • (1998) Proc. Natl. Acad. Sci. USA , vol.95 , pp. 2727-2730
    • Ciechanover, A.1    Schwartz, A.L.2
  • 7
    • 3242665372 scopus 로고    scopus 로고
    • The ubiquitin 26s proteasome proteolytic pathway
    • J. Smalle, and R.D. Vierstra The ubiquitin 26s proteasome proteolytic pathway Annu. Rev. Plant Biol. 55 2004 555 590
    • (2004) Annu. Rev. Plant Biol. , vol.55 , pp. 555-590
    • Smalle, J.1    Vierstra, R.D.2
  • 8
    • 67249143569 scopus 로고    scopus 로고
    • Plants UPS: A database of plants' ubiquitin proteasome system
    • Z. Du, X. Zhou, L. Li, and Z. Su Plants UPS: A database of plants' ubiquitin proteasome system BMC Genomics 10 2009 227
    • (2009) BMC Genomics , vol.10 , pp. 227
    • Du, Z.1    Zhou, X.2    Li, L.3    Su, Z.4
  • 9
    • 38949212916 scopus 로고    scopus 로고
    • Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology
    • M. Windheim, M. Peggie, and P. Cohen Two different classes of E2 ubiquitin-conjugating enzymes are required for the mono-ubiquitination of proteins and elongation by polyubiquitin chains with a specific topology Biochem. J. 409 2008 723 729
    • (2008) Biochem. J. , vol.409 , pp. 723-729
    • Windheim, M.1    Peggie, M.2    Cohen, P.3
  • 10
    • 67349132223 scopus 로고    scopus 로고
    • Physiological functions of the HECT family of ubiquitin ligases
    • D. Rotin, and S. Kumar Physiological functions of the HECT family of ubiquitin ligases Nat. Rev. Mol. Cell Biol. 10 2009 398 409
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 398-409
    • Rotin, D.1    Kumar, S.2
  • 13
    • 64949084332 scopus 로고    scopus 로고
    • The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates
    • D. Yee, and D.R. Goring The diversity of plant U-box E3 ubiquitin ligases: from upstream activators to downstream target substrates J. Exp. Bot. 60 2009 1109 1121
    • (2009) J. Exp. Bot. , vol.60 , pp. 1109-1121
    • Yee, D.1    Goring, D.R.2
  • 14
    • 64949103026 scopus 로고    scopus 로고
    • Classification, expression pattern, and E3 ligase activity assay of rice U-box-containing proteins
    • L.R. Zeng, C.H. Park, R.C. Venu, J. Gough, and G.L. Wang Classification, expression pattern, and E3 ligase activity assay of rice U-box-containing proteins Mol. Plant 1 2008 800 815
    • (2008) Mol. Plant , vol.1 , pp. 800-815
    • Zeng, L.R.1    Park, C.H.2    Venu, R.C.3    Gough, J.4    Wang, G.L.5
  • 15
    • 53749090930 scopus 로고    scopus 로고
    • Interactions between the S-domain receptor kinases and AtPUB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis
    • M.A. Samuel, Y. Mudgil, J.N. Salt, F. Delmas, S. Ramachandran, A. Chilelli, and D.R. Goring Interactions between the S-domain receptor kinases and AtPUB-ARM E3 ubiquitin ligases suggest a conserved signaling pathway in Arabidopsis Plant Physiol. 147 2008 2084 2095
    • (2008) Plant Physiol. , vol.147 , pp. 2084-2095
    • Samuel, M.A.1    Mudgil, Y.2    Salt, J.N.3    Delmas, F.4    Ramachandran, S.5    Chilelli, A.6    Goring, D.R.7
  • 16
    • 84865846468 scopus 로고    scopus 로고
    • Roles of four Arabidopsis U-box E3 ubiquitin ligases in negative regulation of abscisic acid-mediated drought stress responses
    • D.H. Seo, M.Y. Ryu, F. Jammes, J.H. Hwang, M. Turek, B.G. Kang, J.M. Kwak, and W.T. Kim Roles of four Arabidopsis U-box E3 ubiquitin ligases in negative regulation of abscisic acid-mediated drought stress responses Plant Physiol. 160 2012 556 568
    • (2012) Plant Physiol. , vol.160 , pp. 556-568
    • Seo, D.H.1    Ryu, M.Y.2    Jammes, F.3    Hwang, J.H.4    Turek, M.5    Kang, B.G.6    Kwak, J.M.7    Kim, W.T.8
  • 17
    • 84876010099 scopus 로고    scopus 로고
    • The U-box E3 ubiquitin ligase TUD1 functions with a heterotrimeric G α subunit to regulate Brassinosteroid-mediated growth in rice
    • X. Hu, Q. Qian, T. Xu, Y. Zhang, G. Dong, T. Gao, Q. Xie, and Y. Xue The U-box E3 ubiquitin ligase TUD1 functions with a heterotrimeric G α subunit to regulate Brassinosteroid-mediated growth in rice PLoS Genet. 9 2013 e1003391
    • (2013) PLoS Genet. , vol.9 , pp. 1003391
    • Hu, X.1    Qian, Q.2    Xu, T.3    Zhang, Y.4    Dong, G.5    Gao, T.6    Xie, Q.7    Xue, Y.8
  • 18
    • 57749121498 scopus 로고    scopus 로고
    • Arabidopsis PUB22 and PUB23 are homologous U-box E3 ubiquitin ligases that play combinatory roles in response to drought stress
    • S.K. Cho, M.Y. Ryu, C. Song, J.M. Kwak, and W.T. Kim Arabidopsis PUB22 and PUB23 are homologous U-box E3 ubiquitin ligases that play combinatory roles in response to drought stress Plant Cell 20 2008 1899 1914
    • (2008) Plant Cell , vol.20 , pp. 1899-1914
    • Cho, S.K.1    Ryu, M.Y.2    Song, C.3    Kwak, J.M.4    Kim, W.T.5
  • 19
    • 78651399515 scopus 로고    scopus 로고
    • OsPUB15, an E3 ubiquitin ligase, functions to reduce cellular oxidative stress during seed germination
    • J.-J. Park, J. Yi, J. Yoon, J. Ping, H.J. Jeong, S.K. Cho, W.T. Kim, and G. An OsPUB15, an E3 ubiquitin ligase, functions to reduce cellular oxidative stress during seed germination Plant J. 65 2011 194 205
    • (2011) Plant J. , vol.65 , pp. 194-205
    • Park, J.-J.1    Yi, J.2    Yoon, J.3    Ping, J.4    Jeong, H.J.5    Cho, S.K.6    Kim, W.T.7    An, G.8
  • 20
    • 14644422554 scopus 로고    scopus 로고
    • Spotted leaf11, a negative regulator of plant cell death and defense, encodes a U-box/armadillo repeat protein endowed with E3 ubiquitin ligase activity
    • L.-R. Zeng, S. Qu, A. Bordeos, C. Yang, M. Baraoidan, H. Yan, Q. Xie, B.H. Nahm, H. Leung, and G.-L. Wang Spotted leaf11, a negative regulator of plant cell death and defense, encodes a U-box/armadillo repeat protein endowed with E3 ubiquitin ligase activity Plant cell 16 2004 2795 2808
    • (2004) Plant cell , vol.16 , pp. 2795-2808
    • Zeng, L.-R.1    Qu, S.2    Bordeos, A.3    Yang, C.4    Baraoidan, M.5    Yan, H.6    Xie, Q.7    Nahm, B.H.8    Leung, H.9    Wang, G.-L.10
  • 21
    • 84871859886 scopus 로고    scopus 로고
    • The ARC1 E3 ligase gene is frequently deleted in self-compatible Brassicaceae species and has a conserved role in Arabidopsis lyrata self-pollen rejection
    • E. Indriolo, P. Tharmapalan, S.I. Wright, and D.R. Goring The ARC1 E3 ligase gene is frequently deleted in self-compatible Brassicaceae species and has a conserved role in Arabidopsis lyrata self-pollen rejection Plant Cell 24 2012 4607 4620
    • (2012) Plant Cell , vol.24 , pp. 4607-4620
    • Indriolo, E.1    Tharmapalan, P.2    Wright, S.I.3    Goring, D.R.4
  • 22
    • 57749104147 scopus 로고    scopus 로고
    • SPIN1, a K homology domain protein negatively regulated and ubiquitinated by the E3 ubiquitin ligase SPL11, is involved in flowering time control in rice
    • M.E. Vega-Sánchez, L. Zeng, S. Chen, H. Leung, and G.L. Wang SPIN1, a K homology domain protein negatively regulated and ubiquitinated by the E3 ubiquitin ligase SPL11, is involved in flowering time control in rice Plant Cell 20 2008 1456 1469
    • (2008) Plant Cell , vol.20 , pp. 1456-1469
    • Vega-Sánchez, M.E.1    Zeng, L.2    Chen, S.3    Leung, H.4    Wang, G.L.5
  • 23
    • 84877646781 scopus 로고    scopus 로고
    • The N-terminal tetra-peptide (IPDE) short extension of the U-box motif in rice SPL11 E3 is essential for the interaction with E2 and ubiquitin-ligase activity
    • H. Bae, and W.T. Kim The N-terminal tetra-peptide (IPDE) short extension of the U-box motif in rice SPL11 E3 is essential for the interaction with E2 and ubiquitin-ligase activity Biochem. Biophys. Res. Commun. 433 2013 266 271
    • (2013) Biochem. Biophys. Res. Commun. , vol.433 , pp. 266-271
    • Bae, H.1    Kim, W.T.2
  • 24
    • 33644993733 scopus 로고    scopus 로고
    • Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis
    • E. Kraft, S.L. Stone, L. Ma, N. Su, Y. Gao, O.S. Lau, X.W. Deng, and J. Callis Genome analysis and functional characterization of the E2 and RING-type E3 ligase ubiquitination enzymes of Arabidopsis Plant Physiol. 139 2005 1597 1611
    • (2005) Plant Physiol. , vol.139 , pp. 1597-1611
    • Kraft, E.1    Stone, S.L.2    Ma, L.3    Su, N.4    Gao, Y.5    Lau, O.S.6    Deng, X.W.7    Callis, J.8
  • 25
    • 0023375195 scopus 로고
    • The neighbor-joining method: A new method for reconstructing phylogenetic trees
    • N. Saitou, and M. Nei The neighbor-joining method: A new method for reconstructing phylogenetic trees Mol. Biol. Evol. 4 1987 406 425
    • (1987) Mol. Biol. Evol. , vol.4 , pp. 406-425
    • Saitou, N.1    Nei, M.2
  • 26
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • K. Tamura, D. Peterson, N. Peterson, G. Stecher, M. Nei, and S. Kumar MEGA5: Molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods Mol. Biol. Evol. 28 2011 2731 2739
    • (2011) Mol. Biol. Evol. , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5    Kumar, S.6
  • 27
    • 84887566560 scopus 로고    scopus 로고
    • Establishment and application of the yeast two-hybrid (Y2H)-based plant interactome for investigation of gene functions
    • B. Bang, J. Park, J.-S. Jeon, and Y.-S. Seo Establishment and application of the yeast two-hybrid (Y2H)-based plant interactome for investigation of gene functions J. Plant Biol. 56 2013 367 374
    • (2013) J. Plant Biol. , vol.56 , pp. 367-374
    • Bang, B.1    Park, J.2    Jeon, J.-S.3    Seo, Y.-S.4
  • 28
    • 84862803393 scopus 로고    scopus 로고
    • Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and AtRDUF2, reduces tolerance to ABA-mediated drought stress
    • S.J. Kim, M.Y. Ryu, and W.T. Kim Suppression of Arabidopsis RING-DUF1117 E3 ubiquitin ligases, AtRDUF1 and AtRDUF2, reduces tolerance to ABA-mediated drought stress Biochem. Biophys. Res. Commun. 420 2012 141 147
    • (2012) Biochem. Biophys. Res. Commun. , vol.420 , pp. 141-147
    • Kim, S.J.1    Ryu, M.Y.2    Kim, W.T.3
  • 29
    • 67449091213 scopus 로고    scopus 로고
    • What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor?
    • C. Michelle, P. Vourc'h, L. Mignon, and C.R. Andres What was the set of ubiquitin and ubiquitin-like conjugating enzymes in the eukaryote common ancestor? J. Mol. Evol. 68 2009 616 628
    • (2009) J. Mol. Evol. , vol.68 , pp. 616-628
    • Michelle, C.1    Vourc'h, P.2    Mignon, L.3    Andres, C.R.4
  • 31
    • 0035875079 scopus 로고    scopus 로고
    • Molecular insights into polyubiquitinchain assembly: Crystal structure of the Mms2/Ubc13heterodimer
    • A.P. VanDemark, R.M. Hofmann, C. Tsui, C.M. Pickart, and C. Wolberger Molecular insights into polyubiquitinchain assembly: Crystal structure of the Mms2/Ubc13heterodimer Cell 105 2001 711 720
    • (2001) Cell , vol.105 , pp. 711-720
    • Vandemark, A.P.1    Hofmann, R.M.2    Tsui, C.3    Pickart, C.M.4    Wolberger, C.5
  • 33
    • 79959988694 scopus 로고    scopus 로고
    • LEAF TIP NECROSIS1 plays a pivotal role in the regulation of multiple phosphate starvation responses in rice
    • B. Hu, C. Zhu, F. Li, J. Tang, Y. Wang, A. Lin, L. Liu, R. Che, and C. Chu LEAF TIP NECROSIS1 plays a pivotal role in the regulation of multiple phosphate starvation responses in rice Plant Physiol. 156 2011 1101 1115
    • (2011) Plant Physiol. , vol.156 , pp. 1101-1115
    • Hu, B.1    Zhu, C.2    Li, F.3    Tang, J.4    Wang, Y.5    Lin, A.6    Liu, L.7    Che, R.8    Chu, C.9
  • 37
    • 62149103011 scopus 로고    scopus 로고
    • Effect of Arabidopsis COP10 ubiquitin E2 enhancement activity across E2 families and functional conservation among its canonical homologues
    • O.S. Lau, and X.W. Deng Effect of Arabidopsis COP10 ubiquitin E2 enhancement activity across E2 families and functional conservation among its canonical homologues Biochem. J. 418 2009 683 690
    • (2009) Biochem. J. , vol.418 , pp. 683-690
    • Lau, O.S.1    Deng, X.W.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.