메뉴 건너뛰기




Volumn 287, Issue 21, 2012, Pages 17297-17307

Dual role of the molybdenum cofactor biosynthesis protein MOCS3 in tRNA thiolation and molybdenum cofactor biosynthesis in humans

Author keywords

[No Author keywords available]

Indexed keywords

ADENYLATION; C TERMINUS; CELLULAR LOCALIZATION; CYAN FLUORESCENT PROTEIN; CYTOSOLS; DUAL ROLE; ENHANCED YELLOW FLUORESCENT PROTEINS; FLUORESCENCE RESONANCE ENERGY TRANSFER; HUMAN CELLS; MOLYBDENUM-COFACTOR; N-TERMINALS; SULFUR TRANSFER; THIOCARBOXYLATE; THIOLATION;

EID: 84861216122     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.351429     Document Type: Article
Times cited : (44)

References (43)
  • 1
    • 67349193285 scopus 로고    scopus 로고
    • Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes
    • Striebel, F., Imkamp, F., Sutter, M., Steiner, M., Mamedov, A., and Weber- Ban, E. (2009) Bacterial ubiquitin-like modifier Pup is deamidated and conjugated to substrates by distinct but homologous enzymes. Nat. Struct. Mol. Biol. 16, 647-651
    • (2009) Nat. Struct. Mol. Biol. , vol.16 , pp. 647-651
    • Striebel, F.1    Imkamp, F.2    Sutter, M.3    Steiner, M.4    Mamedov, A.5    Weber-Ban, E.6
  • 4
    • 0035891318 scopus 로고    scopus 로고
    • Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex
    • DOI 10.1038/35104586
    • Lake, M. W., Wuebbens, M. M., Rajagopalan, K. V., and Schindelin, H. (2001) Mechanism of ubiquitin activation revealed by the structure of a bacterial MoeB-MoaD complex. Nature 414, 325-329 (Pubitemid 33097811)
    • (2001) Nature , vol.414 , Issue.6861 , pp. 325-329
    • Lake, M.W.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 5
    • 45749124348 scopus 로고    scopus 로고
    • The sulfurtransferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins
    • DOI 10.1021/bi800477u
    • Schmitz, J., Chowdhury, M. M., Hänzelmann, P., Nimtz, M., Lee, E. Y., Schindelin, H., and Leimkühler, S. (2008) The sulfur transferase activity of Uba4 presents a link between ubiquitin-like protein conjugation and activation of sulfur carrier proteins. Biochemistry 47, 6479-6489 (Pubitemid 351874239)
    • (2008) Biochemistry , vol.47 , Issue.24 , pp. 6479-6489
    • Schmitz, J.1    Chowdhury, M.M.2    Hanzelmann, P.3    Nimtz, M.4    Lee, E.-Y.5    Schindelin, H.6    Leimkuhler, S.7
  • 6
    • 45749149275 scopus 로고    scopus 로고
    • Mayer, J. R., Ciechanover, A., Rechsteiner, M., eds Wiley-VCH Verlag, Weinheim, Germany
    • Schindelin, H. (2005) in Protein Degradation 1. Ubiquitin and the Chemistry of Life (Mayer, J. R., Ciechanover, A., Rechsteiner, M., eds) Vol. 1, pp. 21-43, Wiley-VCH Verlag, Weinheim, Germany
    • (2005) Protein Degradation 1. Ubiquitin and the Chemistry of Life , vol.1 , pp. 21-43
    • Schindelin, H.1
  • 7
    • 79952752115 scopus 로고    scopus 로고
    • Molybdenum enzymes in higher organisms
    • Hille, R., Nishino, T., and Bittner, F. (2011) Molybdenum enzymes in higher organisms. Coord. Chem. Rev. 255, 1179-1205
    • (2011) Coord. Chem. Rev. , vol.255 , pp. 1179-1205
    • Hille, R.1    Nishino, T.2    Bittner, F.3
  • 8
    • 0038168025 scopus 로고    scopus 로고
    • Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency
    • DOI 10.1074/jbc.M303092200
    • Leimkuhler, S., Freuer, A., Araujo, J. A., Rajagopalan, K. V., and Mendel, R. R. (2003) Mechanistic studies of human molybdopterin synthase reaction and characterization of mutants identified in group B patients of molybdenum cofactor deficiency. J. Biol. Chem. 278, 26127-26134 (Pubitemid 36835382)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 26127-26134
    • Leimkuhler, S.1    Freuer, A.2    Araujo, J.A.S.3    Rajagopalan, K.V.4    Mendel, R.R.5
  • 9
    • 4344595102 scopus 로고    scopus 로고
    • Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae
    • DOI 10.1074/jbc.M406516200
    • Mühlenhoff, U., Balk, J., Richhardt, N., Kaiser, J. T., Sipos, K., Kispal, G., and Lill, R. (2004) Functional characterization of the eukaryotic cysteine desulfurase Nfs1p from Saccharomyces cerevisiae. J. Biol. Chem. 279, 36906-36915 (Pubitemid 39129040)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.35 , pp. 36906-36915
    • Muhlenhoff, U.1    Balk, J.2    Richhardt, N.3    Kaiser, J.T.4    Sipos, K.5    Kispal, G.6    Lill, R.7
  • 11
    • 54449085541 scopus 로고    scopus 로고
    • A novel role for human Nfs1 in the cytoplasm. Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis
    • Marelja, Z., Stöcklein, W., Nimtz, M., and Leimkühler, S. (2008) A novel role for human Nfs1 in the cytoplasm. Nfs1 acts as a sulfur donor for MOCS3, a protein involved in molybdenum cofactor biosynthesis. J. Biol. Chem. 283, 25178-25185
    • (2008) J. Biol. Chem. , vol.283 , pp. 25178-25185
    • Marelja, Z.1    Stöcklein, W.2    Nimtz, M.3    Leimkühler, S.4
  • 12
    • 79952129481 scopus 로고    scopus 로고
    • Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress
    • Petroski, M. D., Salvesen, G. S., and Wolf, D. A. (2011) Urm1 couples sulfur transfer to ubiquitin-like protein function in oxidative stress. Proc. Natl. Acad. Sci. U.S.A. 108, 1749-1750
    • (2011) Proc. Natl. Acad. Sci. U.S.A. , vol.108 , pp. 1749-1750
    • Petroski, M.D.1    Salvesen, G.S.2    Wolf, D.A.3
  • 13
    • 57449121400 scopus 로고    scopus 로고
    • Afunctional proteomics approach links the ubiquitinrelated modifier Urm1 to a tRNA modification pathway
    • Schlieker, C. D., Van der Veen, A. G., Damon, J. R., Spooner, E., and Ploegh, H. L. (2008)Afunctional proteomics approach links the ubiquitinrelated modifier Urm1 to a tRNA modification pathway. Proc. Natl. Acad. Sci. U.S.A. 105, 18255-18260
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 18255-18260
    • Schlieker, C.D.1    Van Der Veen, A.G.2    Damon, J.R.3    Spooner, E.4    Ploegh, H.L.5
  • 16
    • 62549117409 scopus 로고    scopus 로고
    • Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions
    • Noma, A., Sakaguchi, Y., and Suzuki, T. (2009) Mechanistic characterization of the sulfur-relay system for eukaryotic 2-thiouridine biogenesis at tRNA wobble positions. Nucleic Acids Res. 37, 1335-1352
    • (2009) Nucleic Acids Res. , vol.37 , pp. 1335-1352
    • Noma, A.1    Sakaguchi, Y.2    Suzuki, T.3
  • 17
    • 34147210386 scopus 로고    scopus 로고
    • Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway
    • DOI 10.1128/MCB.01321-06
    • Nakai, Y., Nakai, M., Lill, R., Suzuki, T., and Hayashi, H. (2007) Thio modification of yeast cytosolic tRNA is an iron-sulfur protein-dependent pathway. Mol. Cell. Biol. 27, 2841-2847 (Pubitemid 46581300)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.8 , pp. 2841-2847
    • Nakai, Y.1    Nakai, M.2    Lill, R.3    Suzuki, T.4    Hayashi, H.5
  • 18
    • 0034677757 scopus 로고    scopus 로고
    • A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes
    • DOI 10.1074/jbc.275.11.7462
    • Furukawa, K., Mizushima, N., Noda, T., and Ohsumi, Y. (2000) A protein conjugation system in yeast with homology to biosynthetic enzyme reaction of prokaryotes. J. Biol. Chem. 275, 7462-7465 (Pubitemid 30159639)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.11 , pp. 7462-7465
    • Furukawa, K.1    Mizushima, N.2    Noda, T.3    Ohsumi, Y.4
  • 19
    • 0142216125 scopus 로고    scopus 로고
    • Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p
    • DOI 10.1128/EC.2.5.930-936.2003
    • Goehring, A. S., Rivers, D. M., and Sprague, G. F., Jr. (2003) Attachment of the ubiquitin-related protein Urm1p to the antioxidant protein Ahp1p. Eukaryot. Cell 2, 930-936 (Pubitemid 37298706)
    • (2003) Eukaryotic Cell , vol.2 , Issue.5 , pp. 930-936
    • Goehring, A.S.1    Rivers, D.M.2    Sprague Jr., G.F.3
  • 21
    • 30144434909 scopus 로고    scopus 로고
    • Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis
    • DOI 10.1021/bi051502y
    • Lehmann, C., Begley, T. P., and Ealick, S. E. (2006) Structure of the Escherichia coli ThiS-ThiF complex, a key component of the sulfur transfer system in thiamin biosynthesis. Biochemistry 45, 11-19 (Pubitemid 43054078)
    • (2006) Biochemistry , vol.45 , Issue.1 , pp. 11-19
    • Lehmann, C.1    Begley, T.P.2    Ealick, S.E.3
  • 22
    • 0035167185 scopus 로고    scopus 로고
    • Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation
    • DOI 10.1038/83034
    • Rudolph, M. J., Wuebbens, M. M., Rajagopalan, K. V., and Schindelin, H. (2001) Crystal structure of molybdopterin synthase and its evolutionary relationship to ubiquitin activation. Nat. Struct. Biol. 8, 42-46 (Pubitemid 32043026)
    • (2001) Nature Structural Biology , vol.8 , Issue.1 , pp. 42-46
    • Rudolph, M.J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Schindelin, H.4
  • 24
    • 0038190972 scopus 로고    scopus 로고
    • Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis
    • DOI 10.1074/jbc.M300453200
    • Wuebbens, M. M., and Rajagopalan, K. V. (2003) Mechanistic and mutational studies of Escherichia coli molybdopterin synthase clarify the final step of molybdopterin biosynthesis. J. Biol. Chem. 278, 14523-14532 (Pubitemid 36800006)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.16 , pp. 14523-14532
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 25
    • 0032958546 scopus 로고    scopus 로고
    • Green fluorescent protein as a selectable marker of fibronectin- facilitated retroviral gene transfer in primary human T lymphocytes
    • DOI 10.1089/10430349950019147
    • Dardalhon, V., Noraz, N., Pollok, K., Rebouissou, C., Boyer, M., Bakker, A. Q., Spits, H., and Taylor, N. (1999) Green fluorescent protein as a selectable marker of fibronectin-facilitated retroviral gene transfer in primary human T lymphocytes. Hum. Gene Ther. 10, 5-14 (Pubitemid 29046141)
    • (1999) Human Gene Therapy , vol.10 , Issue.1 , pp. 5-14
    • Dardalhon, V.1    Noraz, N.2    Pollok, K.3    Rebouissou, C.4    Boyer, M.5    Bakker, A.Q.6    Spits, H.7    Taylor, N.8
  • 26
    • 0021333871 scopus 로고
    • The pterin component of the molybdenum factor. Structural characterization of two fluorescent derivatives
    • Johnson, J. L., Hainline, B. E., Rajagopalan, K. V., and Arison, B. H. (1984) The pterin component of the molybdenum cofactor. Structural characterization of two fluorescent derivatives. J. Biol. Chem. 259, 5414-5422 (Pubitemid 14144992)
    • (1984) Journal of Biological Chemistry , vol.259 , Issue.9 , pp. 5414-5422
    • Johnson, J.L.1    Hainline, B.E.2    Rajagopalan, K.V.3    Arison, B.H.4
  • 27
    • 33846392698 scopus 로고    scopus 로고
    • Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold
    • DOI 10.1021/bi062011w
    • Schmitz, J., Wuebbens, M. M., Rajagopalan, K. V., and Leimkühler, S. (2007) Role of the C-terminal Gly-Gly motif of Escherichia coli MoaD, a molybdenum cofactor biosynthesis protein with a ubiquitin fold. Biochemistry 46, 909-916 (Pubitemid 46133607)
    • (2007) Biochemistry , vol.46 , Issue.3 , pp. 909-916
    • Schmitz, J.1    Wuebbens, M.M.2    Rajagopalan, K.V.3    Leimkuhler, S.4
  • 28
    • 0028819468 scopus 로고
    • Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies
    • Wuebbens, M. M., and Rajagopalan, K. V. (1995) Investigation of the early steps of molybdopterin biosynthesis in Escherichia coli through the use of in vivo labeling studies. J. Biol. Chem. 270, 1082-1087
    • (1995) J. Biol. Chem. , vol.270 , pp. 1082-1087
    • Wuebbens, M.M.1    Rajagopalan, K.V.2
  • 29
    • 0000196317 scopus 로고
    • A colorimetric method for the determination of thiosulfate
    • Sörbo, B. (1957) A colorimetric method for the determination of thiosulfate. Biochim. Biophys. Acta 23, 412-416
    • (1957) Biochim. Biophys. Acta , vol.23 , pp. 412-416
    • Sörbo, B.1
  • 30
    • 0019935329 scopus 로고
    • Quantitative enzymatic hydrolysis of tRNAs. Reversed-phase high-performance liquid chromatography of tRNA nucleosides
    • Gehrke, C. W., Kuo, K. C., McCune, R. A., and Gerhardt, K. (1982) Quantitative enzymatic hydrolysis of tRNAs. Reversed-phase high performance liquid chromatography of tRNA nucleosides. J. Chromatogr. 230, 297-308 (Pubitemid 12058025)
    • (1982) Journal of Chromatography , vol.230 , Issue.2 , pp. 297-308
    • Gehrke, C.W.1    Kuo, K.C.2    McCune, R.A.3
  • 31
    • 34249278086 scopus 로고    scopus 로고
    • Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3: Major differences in substrate specificity between eukaryotic and bacterial homologs
    • DOI 10.1111/j.1742-4658.2007.05811.x
    • Krepinsky, K., and Leimkühler, S. (2007) Site-directed mutagenesis of the active site loop of the rhodanese-like domain of the human molybdopterin synthase sulfurase MOCS3. Major differences in substrate specificity between eukaryotic and bacterial homologs. FEBS J. 274, 2778-2787 (Pubitemid 46804939)
    • (2007) FEBS Journal , vol.274 , Issue.11 , pp. 2778-2787
    • Krepinsky, K.1    Leimkuhler, S.2
  • 32
    • 0035860726 scopus 로고    scopus 로고
    • Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor
    • Leimkühler, S., Wuebbens, M. M., and Rajagopalan, K. V. (2001) Characterization of Escherichia coli MoeB and its involvement in the activation of molybdopterin synthase for the biosynthesis of the molybdenum cofactor. J. Biol. Chem. 276, 34695-34701
    • (2001) J. Biol. Chem. , vol.276 , pp. 34695-34701
    • Leimkühler, S.1    Wuebbens, M.M.2    Rajagopalan, K.V.3
  • 34
    • 0020478687 scopus 로고
    • "Covalent affinity" purification of ubiquitin-activating enzyme
    • Ciechanover, A., Elias, S., Heller, H., and Hershko, A. (1982) "Covalent affinity" purification of ubiquitin-activating enzyme. J. Biol. Chem. 257, 2537-2542
    • (1982) J. Biol. Chem. , vol.257 , pp. 2537-2542
    • Ciechanover, A.1    Elias, S.2    Heller, H.3    Hershko, A.4
  • 35
    • 1842424983 scopus 로고    scopus 로고
    • An improved cyan fluorescent protein variant useful for FRET
    • DOI 10.1038/nbt945
    • Rizzo, M. A., Springer, G. H., Granada, B., and Piston, D. W. (2004) An improved cyan fluorescent protein variant useful for FRET. Nat. Biotechnol. 22, 445-449 (Pubitemid 38451376)
    • (2004) Nature Biotechnology , vol.22 , Issue.4 , pp. 445-449
    • Rizzo, M.A.1    Springer, G.H.2    Granada, B.3    Piston, D.W.4
  • 36
    • 0028235968 scopus 로고
    • Substrate properties of site-specific mutant ubiquitin protein (G76a) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1)
    • Pickart, C. M., Kasperek, E. M., Beal, R., and Kim, A. (1994) Substrate properties of site-specific mutant ubiquitin protein (G76A) reveal unexpected mechanistic features of ubiquitin-activating enzyme (E1). J. Biol. Chem. 269, 7115-7123 (Pubitemid 24217895)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.10 , pp. 7115-7123
    • Pickart, C.M.1    Kasperek, E.M.2    Beal, R.3    Kim, A.4
  • 37
    • 77949523576 scopus 로고    scopus 로고
    • Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors
    • Kodiha, M., Tran, D., Morogan, A., Qian, C., and Stochaj, U. (2009) Dissecting the signaling events that impact classical nuclear import and target nuclear transport factors. PLoS One 4, e8420
    • (2009) PLoS One , vol.4
    • Kodiha, M.1    Tran, D.2    Morogan, A.3    Qian, C.4    Stochaj, U.5
  • 38
    • 0030787802 scopus 로고    scopus 로고
    • Antisense inhibition of CAS, the human homologue of the yeast chromosome segregation gene CSE1, interferes with mitosis in HeLa cells
    • DOI 10.1021/bi970236o
    • Ogryzko, V. V., Brinkmann, E., Howard, B. H., Pastan, I., and Brinkmann, U. (1997) Antisense inhibition of CAS, the human homologue of the yeast chromosome segregation gene CSE1, interferes with mitosis in HeLa cells. Biochemistry 36, 9493-9500 (Pubitemid 27346989)
    • (1997) Biochemistry , vol.36 , Issue.31 , pp. 9493-9500
    • Ogryzko, V.V.1    Brinkmann, E.2    Howard, B.H.3    Pastan, I.4    Brinkmann, U.5
  • 39
    • 29544452864 scopus 로고    scopus 로고
    • Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions
    • DOI 10.1016/j.molcel.2005.11.001, PII S1097276505017612
    • Ikeuchi, Y., Shigi, N., Kato, J., Nishimura, A., and Suzuki, T. (2006) Mechanistic insights into sulfur relay by multiple sulfur mediators involved in thiouridine biosynthesis at tRNA wobble positions. Mol. Cell 21, 97-108 (Pubitemid 43017852)
    • (2006) Molecular Cell , vol.21 , Issue.1 , pp. 97-108
    • Ikeuchi, Y.1    Shigi, N.2    Kato, J.-I.3    Nishimura, A.4    Suzuki, T.5
  • 40
    • 78249261631 scopus 로고    scopus 로고
    • Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegans
    • Kim, S., Johnson, W., Chen, C., Sewell, A. K., Byström, A. S., and Han, M. (2010) Allele-specific suppressors of lin-1(R175Opal) identify functions of MOC-3 and DPH-3 in tRNA modification complexes in Caenorhabditis elegans. Genetics 185, 1235-1247
    • (2010) Genetics , vol.185 , pp. 1235-1247
    • Kim, S.1    Johnson, W.2    Chen, C.3    Sewell, A.K.4    Byström, A.S.5    Han, M.6
  • 41
    • 78650318976 scopus 로고    scopus 로고
    • The yeast ubiquitin-like domain protein Mdy2 is required for microtubule- directed nuclear migration and localizes to cytoplasmic granules in response to heat stress
    • Cohnen, A., Bielig, H., Hollenberg, C. P., Hu, Z., and Ramezani-Rad, M. (2010) The yeast ubiquitin-like domain protein Mdy2 is required for microtubule- directed nuclear migration and localizes to cytoplasmic granules in response to heat stress. Cytoskeleton 67, 635-649
    • (2010) Cytoskeleton , vol.67 , pp. 635-649
    • Cohnen, A.1    Bielig, H.2    Hollenberg, C.P.3    Hu, Z.4    Ramezani-Rad, M.5
  • 42
    • 0037128207 scopus 로고    scopus 로고
    • SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles
    • DOI 10.1083/jcb.200110109
    • Joseph, J., Tan, S. H., Karpova, T. S., McNally, J. G., and Dasso, M. (2002) SUMO-1 targets RanGAP1 to kinetochores and mitotic spindles. J. Cell Biol. 156, 595-602 (Pubitemid 34839875)
    • (2002) Journal of Cell Biology , vol.156 , Issue.4 , pp. 595-602
    • Joseph, J.1    Tan, S.-H.2    Karpova, T.S.3    McNally, J.G.4    Dasso, M.5
  • 43
    • 0037059619 scopus 로고    scopus 로고
    • The nucleoporin RanBP2 has SUMO1 E3 ligase activity
    • DOI 10.1016/S0092-8674(01)00633-X
    • Pichler, A., Gast, A., Seeler, J. S., Dejean, A., and Melchior, F. (2002) The nucleoporin RanBP2 has SUMO1 E3 ligase activity. Cell 108, 109-120 (Pubitemid 34137016)
    • (2002) Cell , vol.108 , Issue.1 , pp. 109-120
    • Pichler, A.1    Gast, A.2    Seeler, J.S.3    Dejean, A.4    Melchior, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.