메뉴 건너뛰기




Volumn 55, Issue 12, 2016, Pages 1898-1908

A Rapid and Versatile Method for Generating Proteins with Defined Ubiquitin Chains

Author keywords

[No Author keywords available]

Indexed keywords

AMINO ACIDS; BIOSYNTHESIS; CHAINS; COMPLEXATION; MOLECULAR BIOLOGY;

EID: 84962467507     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/acs.biochem.5b01310     Document Type: Article
Times cited : (33)

References (42)
  • 1
    • 84861877407 scopus 로고    scopus 로고
    • The ubiquitin code
    • Komander, D. and Rape, M. (2012) The ubiquitin code Annu. Rev. Biochem. 81, 203-229 10.1146/annurev-biochem-060310-170328
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 203-229
    • Komander, D.1    Rape, M.2
  • 2
    • 70350150000 scopus 로고    scopus 로고
    • The emerging complexity of protein ubiquitination
    • Komander, D. (2009) The emerging complexity of protein ubiquitination Biochem. Soc. Trans. 37, 937-953 10.1042/BST0370937
    • (2009) Biochem. Soc. Trans. , vol.37 , pp. 937-953
    • Komander, D.1
  • 3
    • 0034602845 scopus 로고    scopus 로고
    • Recognition of the polyubiquitin proteolytic signal
    • Thrower, J. S., Hoffman, L., Rechsteiner, M., and Pickart, C. M. (2000) Recognition of the polyubiquitin proteolytic signal EMBO J. 19, 94-102 10.1093/emboj/19.1.94
    • (2000) EMBO J. , vol.19 , pp. 94-102
    • Thrower, J.S.1    Hoffman, L.2    Rechsteiner, M.3    Pickart, C.M.4
  • 4
    • 84879480889 scopus 로고    scopus 로고
    • Non-canonical ubiquitylation: Mechanisms and consequences
    • McDowell, G. S. and Philpott, A. (2013) Non-canonical ubiquitylation: mechanisms and consequences Int. J. Biochem. Cell Biol. 45, 1833-1842 10.1016/j.biocel.2013.05.026
    • (2013) Int. J. Biochem. Cell Biol. , vol.45 , pp. 1833-1842
    • McDowell, G.S.1    Philpott, A.2
  • 5
    • 63049125531 scopus 로고    scopus 로고
    • Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation
    • Xu, P., Duong, D. M., Seyfried, N. T., Cheng, D., Xie, Y., Robert, J., Rush, J., Hochstrasser, M., Finley, D., and Peng, J. (2009) Quantitative proteomics reveals the function of unconventional ubiquitin chains in proteasomal degradation Cell 137, 133-145 10.1016/j.cell.2009.01.041
    • (2009) Cell , vol.137 , pp. 133-145
    • Xu, P.1    Duong, D.M.2    Seyfried, N.T.3    Cheng, D.4    Xie, Y.5    Robert, J.6    Rush, J.7    Hochstrasser, M.8    Finley, D.9    Peng, J.10
  • 6
    • 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., and Vierstra, R. D. (2013) Advanced proteomic analyses yield a deep catalog of ubiquitylation targets in Arabidopsis Plant Cell 25, 1523-1540 10.1105/tpc.112.108613
    • (2013) Plant Cell , vol.25 , pp. 1523-1540
    • Kim, D.-Y.1    Scalf, M.2    Smith, L.M.3    Vierstra, R.D.4
  • 8
    • 0024514688 scopus 로고
    • A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein
    • Chau, V., Tobias, J. W., Bachmair, A., Marriott, D., Ecker, D. J., Gonda, D. K., and Varshavsky, A. (1989) A multiubiquitin chain is confined to specific lysine in a targeted short-lived protein Science 243, 1576-1583 10.1126/science.2538923
    • (1989) Science , vol.243 , pp. 1576-1583
    • Chau, V.1    Tobias, J.W.2    Bachmair, A.3    Marriott, D.4    Ecker, D.J.5    Gonda, D.K.6    Varshavsky, A.7
  • 9
    • 0030881952 scopus 로고    scopus 로고
    • Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein
    • Galan, J. M. and Haguenauer-Tsapis, R. (1997) Ubiquitin lys63 is involved in ubiquitination of a yeast plasma membrane protein EMBO J. 16, 5847-5854 10.1093/emboj/16.19.5847
    • (1997) EMBO J. , vol.16 , pp. 5847-5854
    • Galan, J.M.1    Haguenauer-Tsapis, R.2
  • 10
    • 60549107173 scopus 로고    scopus 로고
    • Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome
    • Saeki, Y., Kudo, T., Sone, T., Kikuchi, Y., Yokosawa, H., Toh-E, A., and Tanaka, K. (2009) Lysine 63-linked polyubiquitin chain may serve as a targeting signal for the 26S proteasome EMBO J. 28, 359-371 10.1038/emboj.2008.305
    • (2009) EMBO J. , vol.28 , pp. 359-371
    • Saeki, Y.1    Kudo, T.2    Sone, T.3    Kikuchi, Y.4    Yokosawa, H.5    Toh-E, A.6    Tanaka, K.7
  • 11
    • 0035958926 scopus 로고    scopus 로고
    • In vitro assembly and recognition of Lys-63 polyubiquitin chains
    • Hofmann, R. M. and Pickart, C. M. (2001) In vitro assembly and recognition of Lys-63 polyubiquitin chains J. Biol. Chem. 276, 27936-27943 10.1074/jbc.M103378200
    • (2001) J. Biol. Chem. , vol.276 , pp. 27936-27943
    • Hofmann, R.M.1    Pickart, C.M.2
  • 12
    • 43049162227 scopus 로고    scopus 로고
    • Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex
    • Jin, L., Williamson, A., Banerjee, S., Philipp, I., and Rape, M. (2008) Mechanism of ubiquitin-chain formation by the human anaphase-promoting complex Cell 133, 653-665 10.1016/j.cell.2008.04.012
    • (2008) Cell , vol.133 , pp. 653-665
    • Jin, L.1    Williamson, A.2    Banerjee, S.3    Philipp, I.4    Rape, M.5
  • 14
    • 84900337781 scopus 로고    scopus 로고
    • Enhanced protein degradation by branched ubiquitin chains
    • Meyer, H.-J. and Rape, M. (2014) Enhanced protein degradation by branched ubiquitin chains Cell 157, 910-921 10.1016/j.cell.2014.03.037
    • (2014) Cell , vol.157 , pp. 910-921
    • Meyer, H.-J.1    Rape, M.2
  • 15
    • 84947045877 scopus 로고    scopus 로고
    • The Proteasome Distinguishes between Heterotypic and Homotypic Lysine-11-Linked Polyubiquitin Chains
    • Grice, G. L., Lobb, I. T., Weekes, M. P., Gygi, S. P., Antrobus, R., and Nathan, J. A. (2015) The Proteasome Distinguishes between Heterotypic and Homotypic Lysine-11-Linked Polyubiquitin Chains Cell Rep. 12, 545-553 10.1016/j.celrep.2015.06.061
    • (2015) Cell Rep. , vol.12 , pp. 545-553
    • Grice, G.L.1    Lobb, I.T.2    Weekes, M.P.3    Gygi, S.P.4    Antrobus, R.5    Nathan, J.A.6
  • 16
    • 84946231682 scopus 로고    scopus 로고
    • The missing links to link ubiquitin: Methods for the enzymatic production of polyubiquitin chains
    • Faggiano, S., Alfano, C., and Pastore, A. (2016) The missing links to link ubiquitin: Methods for the enzymatic production of polyubiquitin chains Anal. Biochem. 492, 82-90 10.1016/j.ab.2015.09.013
    • (2016) Anal. Biochem. , vol.492 , pp. 82-90
    • Faggiano, S.1    Alfano, C.2    Pastore, A.3
  • 17
    • 79551471508 scopus 로고    scopus 로고
    • Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups
    • Castañeda, C. A., Liu, J., Kashyap, T. R., Singh, R. K., Fushman, D., and Cropp, T. A. (2011) Controlled enzymatic synthesis of natural-linkage, defined-length polyubiquitin chains using lysines with removable protecting groups Chem. Commun. 47, 2026-2028 10.1039/c0cc04868b
    • (2011) Chem. Commun. , vol.47 , pp. 2026-2028
    • Castañeda, C.A.1    Liu, J.2    Kashyap, T.R.3    Singh, R.K.4    Fushman, D.5    Cropp, T.A.6
  • 19
    • 28844462033 scopus 로고    scopus 로고
    • Controlled synthesis of polyubiquitin chains
    • Pickart, C. M. and Raasi, S. (2005) Controlled synthesis of polyubiquitin chains Methods Enzymol. 399, 21-36 10.1016/S0076-6879(05)99002-2
    • (2005) Methods Enzymol. , vol.399 , pp. 21-36
    • Pickart, C.M.1    Raasi, S.2
  • 20
    • 20344373955 scopus 로고    scopus 로고
    • Ubiquitin chain synthesis
    • Raasi, S. and Pickart, C. M. (2005) Ubiquitin chain synthesis Methods Mol. Biol. 301, 47-56 10.1385/1-59259-895-1:047
    • (2005) Methods Mol. Biol. , vol.301 , pp. 47-56
    • Raasi, S.1    Pickart, C.M.2
  • 21
    • 28844486027 scopus 로고    scopus 로고
    • In vitro SCFbeta-Trcp1-mediated IkappaBalpha ubiquitination assay for high-throughput screen
    • Xu, S., Patel, P., Abbasian, M., Giegel, D., Xie, W., Mercurio, F., and Cox, S. (2005) In vitro SCFbeta-Trcp1-mediated IkappaBalpha ubiquitination assay for high-throughput screen Methods Enzymol. 399, 729-740 10.1016/S0076-6879(05)99048-4
    • (2005) Methods Enzymol. , vol.399 , pp. 729-740
    • Xu, S.1    Patel, P.2    Abbasian, M.3    Giegel, D.4    Xie, W.5    Mercurio, F.6    Cox, S.7
  • 22
    • 28844484999 scopus 로고    scopus 로고
    • Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity
    • Saeki, Y., Isono, E., and Toh-E, A. (2005) Preparation of ubiquitinated substrates by the PY motif-insertion method for monitoring 26S proteasome activity Methods Enzymol. 399, 215-227 10.1016/S0076-6879(05)99014-9
    • (2005) Methods Enzymol. , vol.399 , pp. 215-227
    • Saeki, Y.1    Isono, E.2    Toh-E, A.3
  • 23
    • 84878245546 scopus 로고    scopus 로고
    • Nonenzymatic assembly of branched polyubiquitin chains for structural and biochemical studies
    • Dixon, E. K., Castañeda, C. A., Kashyap, T. R., Wang, Y., and Fushman, D. (2013) Nonenzymatic assembly of branched polyubiquitin chains for structural and biochemical studies Bioorg. Med. Chem. 21, 3421-3429 10.1016/j.bmc.2013.02.052
    • (2013) Bioorg. Med. Chem. , vol.21 , pp. 3421-3429
    • Dixon, E.K.1    Castañeda, C.A.2    Kashyap, T.R.3    Wang, Y.4    Fushman, D.5
  • 24
    • 84904558632 scopus 로고    scopus 로고
    • Chemoenzymatic Synthesis of Bifunctional Polyubiquitin Substrates for Monitoring Ubiquitin Chain Remodeling
    • Trang, V. H., Rodgers, M. L., Boyle, K. J., Hoskins, A. A., and Strieter, E. R. (2014) Chemoenzymatic Synthesis of Bifunctional Polyubiquitin Substrates for Monitoring Ubiquitin Chain Remodeling ChemBioChem 15, 1563-1568 10.1002/cbic.201402059
    • (2014) ChemBioChem , vol.15 , pp. 1563-1568
    • Trang, V.H.1    Rodgers, M.L.2    Boyle, K.J.3    Hoskins, A.A.4    Strieter, E.R.5
  • 25
    • 84855796716 scopus 로고    scopus 로고
    • Chemical synthesis of ubiquitinated peptides with varying lengths and types of ubiquitin chains to explore the activity of deubiquitinases
    • Bavikar, S. N., Spasser, L., Haj-Yahya, M., Karthikeyan, S. V., Moyal, T., Ajish Kumar, K. S., and Brik, A. (2012) Chemical synthesis of ubiquitinated peptides with varying lengths and types of ubiquitin chains to explore the activity of deubiquitinases Angew. Chem., Int. Ed. 51, 758-763 10.1002/anie.201106430
    • (2012) Angew. Chem., Int. Ed. , vol.51 , pp. 758-763
    • Bavikar, S.N.1    Spasser, L.2    Haj-Yahya, M.3    Karthikeyan, S.V.4    Moyal, T.5    Ajish Kumar, K.S.6    Brik, A.7
  • 26
    • 67650719844 scopus 로고    scopus 로고
    • Semisynthesis of ubiquitylated proteins
    • Mcginty, R. K., Chatterjee, C., and Muir, T. W. (2009) Semisynthesis of ubiquitylated proteins Methods Enzymol. 462, 225-243 10.1016/S0076-6879(09)62011-5
    • (2009) Methods Enzymol. , vol.462 , pp. 225-243
    • McGinty, R.K.1    Chatterjee, C.2    Muir, T.W.3
  • 27
    • 80455123843 scopus 로고    scopus 로고
    • Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme
    • Castañeda, C., Liu, J., Chaturvedi, A., Nowicka, U., Cropp, T. A., and Fushman, D. (2011) Nonenzymatic assembly of natural polyubiquitin chains of any linkage composition and isotopic labeling scheme J. Am. Chem. Soc. 133, 17855-17868 10.1021/ja207220g
    • (2011) J. Am. Chem. Soc. , vol.133 , pp. 17855-17868
    • Castañeda, C.1    Liu, J.2    Chaturvedi, A.3    Nowicka, U.4    Cropp, T.A.5    Fushman, D.6
  • 28
    • 30544433196 scopus 로고    scopus 로고
    • Engineering and characterization of a superfolder green fluorescent protein
    • Pédelacq, J.-D., Cabantous, S., Tran, T., Terwilliger, T. C., and Waldo, G. S. (2006) Engineering and characterization of a superfolder green fluorescent protein Nat. Biotechnol. 24, 79-88 10.1038/nbt1172
    • (2006) Nat. Biotechnol. , vol.24 , pp. 79-88
    • Pédelacq, J.-D.1    Cabantous, S.2    Tran, T.3    Terwilliger, T.C.4    Waldo, G.S.5
  • 29
    • 84875679578 scopus 로고    scopus 로고
    • Engineering fluorescent protein substrates for the AAA+ Lon protease
    • Wohlever, M. L., Nager, A. R., Baker, T. A., and Sauer, R. T. (2013) Engineering fluorescent protein substrates for the AAA+ Lon protease Protein Eng., Des. Sel. 26, 299-305 10.1093/protein/gzs105
    • (2013) Protein Eng., Des. Sel. , vol.26 , pp. 299-305
    • Wohlever, M.L.1    Nager, A.R.2    Baker, T.A.3    Sauer, R.T.4
  • 30
    • 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., and Matouschek, A. (2004) An unstructured initiation site is required for efficient proteasome-mediated degradation Nat. Struct. Mol. Biol. 11, 830-837 10.1038/nsmb814
    • (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
  • 31
    • 84922253993 scopus 로고    scopus 로고
    • Top-down 193-nm ultraviolet photodissociation mass spectrometry for simultaneous determination of polyubiquitin chain length and topology
    • Cannon, J. R., Martinez-Fonts, K., Robotham, S. A., Matouschek, A., and Brodbelt, J. S. (2015) Top-down 193-nm ultraviolet photodissociation mass spectrometry for simultaneous determination of polyubiquitin chain length and topology Anal. Chem. 87, 1812-1820 10.1021/ac5038363
    • (2015) Anal. Chem. , vol.87 , pp. 1812-1820
    • Cannon, J.R.1    Martinez-Fonts, K.2    Robotham, S.A.3    Matouschek, A.4    Brodbelt, J.S.5
  • 33
    • 77955417276 scopus 로고    scopus 로고
    • Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne
    • Bremm, A., Freund, S. M. V., and Komander, D. (2010) Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne Nat. Struct. Mol. Biol. 17, 939-947 10.1038/nsmb.1873
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 939-947
    • Bremm, A.1    Freund, S.M.V.2    Komander, D.3
  • 34
    • 84858175449 scopus 로고    scopus 로고
    • Synthesis and analysis of K11-linked ubiquitin chains
    • Bremm, A. and Komander, D. (2012) Synthesis and analysis of K11-linked ubiquitin chains Methods Mol. Biol. 832, 219-228 10.1007/978-1-61779-474-2-15
    • (2012) Methods Mol. Biol. , vol.832 , pp. 219-228
    • Bremm, A.1    Komander, D.2
  • 36
    • 3042799223 scopus 로고    scopus 로고
    • Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae
    • Sone, T., Saeki, Y., Toh-E, A., and Yokosawa, H. (2004) Sem1p is a novel subunit of the 26 S proteasome from Saccharomyces cerevisiae J. Biol. Chem. 279, 28807-28816 10.1074/jbc.M403165200
    • (2004) J. Biol. Chem. , vol.279 , pp. 28807-28816
    • Sone, T.1    Saeki, Y.2    Toh-E, A.3    Yokosawa, H.4
  • 37
    • 0025644201 scopus 로고
    • A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin
    • Chen, Z. and Pickart, C. M. (1990) A 25-kilodalton ubiquitin carrier protein (E2) catalyzes multi-ubiquitin chain synthesis via lysine 48 of ubiquitin J. Biol. Chem. 265, 21835-21842
    • (1990) J. Biol. Chem. , vol.265 , pp. 21835-21842
    • Chen, Z.1    Pickart, C.M.2
  • 38
    • 0030772445 scopus 로고    scopus 로고
    • Structure and function of ubiquitin conjugating enzyme E2-25K: The tail is a core-dependent activity element
    • Haldeman, M. T., Xia, G., Kasperek, E. M., and Pickart, C. M. (1997) Structure and function of ubiquitin conjugating enzyme E2-25K: the tail is a core-dependent activity element Biochemistry 36, 10526-10537 10.1021/bi970750u
    • (1997) Biochemistry , vol.36 , pp. 10526-10537
    • Haldeman, M.T.1    Xia, G.2    Kasperek, E.M.3    Pickart, C.M.4
  • 39
    • 0033525582 scopus 로고    scopus 로고
    • Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair
    • Hofmann, R. M. and Pickart, C. M. (1999) Noncanonical MMS2-encoded ubiquitin-conjugating enzyme functions in assembly of novel polyubiquitin chains for DNA repair Cell 96, 645-653 10.1016/S0092-8674(00)80575-9
    • (1999) Cell , vol.96 , pp. 645-653
    • Hofmann, R.M.1    Pickart, C.M.2
  • 40
    • 33646066025 scopus 로고    scopus 로고
    • The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin
    • Reyes-Turcu, F. E., Horton, J. R., Mullally, J. E., Heroux, A., Cheng, X., and Wilkinson, K. D. (2006) The ubiquitin binding domain ZnF UBP recognizes the C-terminal diglycine motif of unanchored ubiquitin Cell 124, 1197-1208 10.1016/j.cell.2006.02.038
    • (2006) Cell , vol.124 , pp. 1197-1208
    • Reyes-Turcu, F.E.1    Horton, J.R.2    Mullally, J.E.3    Heroux, A.4    Cheng, X.5    Wilkinson, K.D.6
  • 41
    • 84942543892 scopus 로고    scopus 로고
    • Click chemistry for targeted protein ubiquitylation and ubiquitin chain formation
    • Rösner, D., Schneider, T., Schneider, D., Scheffner, M., and Marx, A. (2015) Click chemistry for targeted protein ubiquitylation and ubiquitin chain formation Nat. Protoc. 10, 1594-1611 10.1038/nprot.2015.106
    • (2015) Nat. Protoc. , vol.10 , pp. 1594-1611
    • Rösner, D.1    Schneider, T.2    Schneider, D.3    Scheffner, M.4    Marx, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.