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Volumn 63, Issue 7, 2011, Pages 457-462

Unraveling moonlighting functions with yeasts

Author keywords

aconitase; hexokinase; moonlighting; pyruvate carboxylase; yeasts

Indexed keywords

6 PHOSPHOFRUCTOKINASE; ACETOHYDROXIACID REDUCTOISOMERASE; ACONITATE HYDRATASE; ADENYLATE KINASE; ALCOHOL OXIDASE; ARGINASE; COENZYME A; CYCLOOXYGENASE 1 INHIBITOR; CYTOCHROME C OXIDASE; ENOLASE; ENZYME; FRUCTOSE BISPHOSPHATE ALDOLASE; GALACTOKINASE; HEXOKINASE 2; INOSITOL P KINASE; IRON SULFUR PROTEIN; LYSINE; METHIONINE; MITOCHONDRIAL DNA; MOONLIGHTING PROTEIN; OXALOACETIC ACID; PROTEIN; PYRUVATE CARBOXYLASE; TRANSCRIPTION FACTOR SNF; UNCLASSIFIED DRUG; WNT2 PROTEIN;

EID: 79959620141     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.454     Document Type: Review
Times cited : (24)

References (40)
  • 2
    • 0033048066 scopus 로고    scopus 로고
    • Moonlighting proteins
    • DOI 10.1016/S0968-0004(98)01335-8, PII S0968000498013358
    • Jeffery, C. J., (1999) Moonlighting proteins. Trends Biochem. Sci. 24, 8-11. (Pubitemid 29074455)
    • (1999) Trends in Biochemical Sciences , vol.24 , Issue.1 , pp. 8-11
    • Jeffery, C.J.1
  • 3
    • 77953623874 scopus 로고    scopus 로고
    • Enzyme promiscuity: A mechanistic and evolutionary perspective
    • Khersonsky, O., and, D. S. Tawfik, (2010) Enzyme promiscuity: a mechanistic and evolutionary perspective. Ann. Rev. Biochem. 79, 471-505.
    • (2010) Ann. Rev. Biochem. , vol.79 , pp. 471-505
    • Khersonsky, O.1    S, T.D.2
  • 4
    • 77950369259 scopus 로고    scopus 로고
    • Moonlighting proteins: An intriguing mode of multitasking
    • Huberts, D. H., and, I. J. van der Klei, (2010) Moonlighting proteins: an intriguing mode of multitasking. Biochim. Biophys. Acta 1803, 520-525.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 520-525
    • Huberts, D.H.1    Van Der Klei, I.J.2
  • 6
    • 0036235651 scopus 로고    scopus 로고
    • The hexokinase 2-dependent glucose signal transduction pathway of Saccharomyces cerevisiae
    • DOI 10.1016/S0168-6445(01)00077-8, PII S0168644501000778
    • Moreno, F., and, P. Herrero, (2002) The hexokinase 2-dependent glucose signal transduction pathway of Saccharomyces cerevisiae. FEMS Microbiol. Rev. 26, 83-90. (Pubitemid 34454777)
    • (2002) FEMS Microbiology Reviews , vol.26 , Issue.1 , pp. 83-90
    • Moreno, F.1    Herrero, P.2
  • 7
    • 78649735310 scopus 로고    scopus 로고
    • Functional domains of yeast hexokinase 2
    • Pelaez, R., P. Herrero., and, F. Moreno, (2010) Functional domains of yeast hexokinase 2. Biochem. J. 432, 181-190.
    • (2010) Biochem. J. , vol.432 , pp. 181-190
    • Pelaez, R.1    Herrero, P.2    Moreno, F.3
  • 8
    • 0037323567 scopus 로고    scopus 로고
    • Pyruvate carboxylase is an essential protein in the assembly of yeast peroxisomal oligomeric alcohol oxidase
    • DOI 10.1091/mbc.E02-07-0417
    • Ozimek, P., R. van Dijk, Latchev, K., Gancedo, C., Wang, D. Y., van der Klei, I. J., and, Veenhuis, M., (2003) Pyruvate carboxylase is an essential protein in the assembly of yeast peroxisomal oligomeric alcohol oxidase. Mol. Biol. Cell. 14, 786-797. (Pubitemid 36237032)
    • (2003) Molecular Biology of the Cell , vol.14 , Issue.2 , pp. 786-797
    • Ozimek, P.1    Van Dijk, R.2    Latchev, K.3    Gancedo, C.4    Wang, D.Y.5    Van Der Klei, I.J.6    Veenhuis, M.7
  • 9
    • 77954957537 scopus 로고    scopus 로고
    • The moonlighting function of pyruvate carboxylase resides in the non-catalytic end of the TIM barrel
    • Huberts, D. H., Venselaar, H.,;, Vriend, G.,;, Veenhuis, M.,; and, van der Klei, I. J., (2010) The moonlighting function of pyruvate carboxylase resides in the non-catalytic end of the TIM barrel. Biochim. Biophys. Acta 1803, 1038-1042.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 1038-1042
    • Huberts, D.H.1    Venselaar, H.2    Vriend, G.3    Veenhuis, M.4    Van Der Klei, I.J.5
  • 10
    • 13244277441 scopus 로고    scopus 로고
    • Aconitase couples metabolic regulation to mitochondrial DNA maintenance
    • DOI 10.1126/science.1106391
    • Chen, X. J., Wang, X., Kaufman, B. A., and, Butow, R. A., (2005) Aconitase couples metabolic regulation to mitochondrial DNA maintenance. Science 307, 714-717. (Pubitemid 40194639)
    • (2005) Science , vol.307 , Issue.5710 , pp. 714-717
    • Xin, J.C.1    Wang, X.2    Kaufman, B.A.3    Butow, R.A.4
  • 12
    • 73549091964 scopus 로고    scopus 로고
    • Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis
    • Ruiz, A., González, A., Muñoz, I., Serrano, R., Abrie, J. A., Strauss, E,. and Arin, J. (2009) Moonlighting proteins Hal3 and Vhs3 form a heteromeric PPCDC with Ykl088w in yeast CoA biosynthesis. Nat. Chem. Biol. 5, 920-928.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 920-928
    • Ruiz, A.1    González, A.2    Muñoz, I.3    Serrano, R.4    Abrie, J.A.5    Strauss, E.6    Arin, J.7
  • 14
    • 0018969294 scopus 로고
    • Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast
    • DOI 10.1007/BF00337871
    • Entian, K. D., (1980) Genetic and biochemical evidence for hexokinase PII as a key enzyme involved in carbon catabolite repression in yeast. Mol. Gen. Genet. 178, 633-637. (Pubitemid 10002920)
    • (1980) Molecular and General Genetics , vol.178 , Issue.3 , pp. 633-637
    • Entian, K.D.1
  • 15
    • 0022815674 scopus 로고
    • Effects of null mutations in the hexokinase genes of Saccharomyces cerevisiae on catabolite repression
    • Ma, H., and, Botstein, D., (1986) Effects of null mutations in the hexokinase genes of Saccharomyces cerevisiae on catabolite repression. Mol. Cell. Biol. 6, 4046-4052.
    • (1986) Mol. Cell. Biol. , vol.6 , pp. 4046-4052
    • Ma, H.1    Botstein, D.2
  • 16
    • 0021266044 scopus 로고
    • Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering carbon catabolite repression
    • Entian, K. D., and, Frohlich, K. U., (1984) Saccharomyces cerevisiae mutants provide evidence of hexokinase PII as a bifunctional enzyme with catalytic and regulatory domains for triggering carbon catabolite repression. J. Bacteriol. 158, 29-35. (Pubitemid 14127469)
    • (1984) Journal of Bacteriology , vol.158 , Issue.1 , pp. 29-35
    • Entian, K.D.1    Frohlich, K.U.2
  • 17
    • 33947493105 scopus 로고    scopus 로고
    • Hxk2 regulates the phosphorylation state of Mig1 and therefore its nucleocytoplasmic distribution
    • DOI 10.1074/jbc.M606854200
    • Ahuatzi, D., Riera, A., Pelaez, R., Herrero, P., and, Moreno, F., (2007) Hxk2 regulates the phosphorylation state of Mig1 and therefore its nucleocytoplasmic distribution. J. Biol. Chem. 282, 4485-4493. (Pubitemid 47100982)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.7 , pp. 4485-4493
    • Ahuatzi, D.1    Riera, A.2    Pelaez, R.3    Herrero, P.4    Moreno, F.5
  • 18
    • 34548589171 scopus 로고    scopus 로고
    • The transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase
    • DOI 10.1111/j.1567-1364.2007.00214.x
    • Ozimek, P. Z., Klompmaker, S. H., Visser, N., Veenhuis, M., and, van der Klei, I. J., (2007) The transcarboxylase domain of pyruvate carboxylase is essential for assembly of the peroxisomal flavoenzyme alcohol oxidase. FEMS Yeast Res. 7, 1082-1092. (Pubitemid 47390285)
    • (2007) FEMS Yeast Research , vol.7 , Issue.7 , pp. 1082-1092
    • Ozimek, P.Z.1    Klompmaker, S.H.2    Visser, N.3    Veenhuis, M.4    Van Der Klei, I.J.5
  • 19
    • 29344442844 scopus 로고    scopus 로고
    • Hansenula polymorpha and Saccharomyces cerevisiae Pex5p's recognize different, independent peroxisomal targeting signals in alcohol oxidase
    • DOI 10.1016/j.febslet.2005.11.045, PII S0014579305014146
    • Ozimek, P., Kotter, P., Veenhuis, M., and, van der Klei, I. J., (2006) Hansenula polymorpha and Saccharomyces cerevisiae Pex5p's recognize different, independent peroxisomal targeting signals in alcohol oxidase. FEBS Lett. 580, 46-50. (Pubitemid 43005310)
    • (2006) FEBS Letters , vol.580 , Issue.1 , pp. 46-50
    • Ozimek, P.1    Kotter, P.2    Veenhuis, M.3    Van Der Klei, I.J.4
  • 20
    • 33746361251 scopus 로고    scopus 로고
    • The role of iron regulatory proteins in mammalian iron homeostasis and disease
    • DOI 10.1038/nchembio807, PII NCHEMBIO807
    • Rouault, T. A., (2006) The role of iron regulatory proteins in mammalian iron homeostasis and disease. Nat. Chem. Biol. 2, 406-414. (Pubitemid 44114917)
    • (2006) Nature Chemical Biology , vol.2 , Issue.8 , pp. 406-414
    • Rouault, T.A.1
  • 21
    • 33745195271 scopus 로고    scopus 로고
    • Yeast Gal4: A transcriptional paradigm revisited
    • DOI 10.1038/sj.embor.7400679, PII 7400679
    • Traven, A., Jelicic, B., and, Sopta, M., (2006) Yeast Gal4: a transcriptional paradigm revisited. EMBO Rep. 7, 496-499. (Pubitemid 43904865)
    • (2006) EMBO Reports , vol.7 , Issue.5 , pp. 496-499
    • Traven, A.1    Jelicic, B.2    Sopta, M.3
  • 22
    • 0034531651 scopus 로고    scopus 로고
    • Iron regulatory proteins in pathobiology
    • DOI 10.1042/0264-6021:3520241
    • Cairo, G., and, Pietrangelo, A., (2000) Iron regulatory proteins in pathobiology. Biochem. J. 352 Pt 2, 241-250. (Pubitemid 32011418)
    • (2000) Biochemical Journal , vol.352 , Issue.2 , pp. 241-250
    • Cairo, G.1    Pietrangelo, A.2
  • 23
    • 69949162863 scopus 로고    scopus 로고
    • Bioinformatics annotation of the hypothetical proteins found by omics techniques can help to disclose additional virulence factors
    • Hernandez, S., Gomez, A., Cedano, J., and, Querol, E., (2009) Bioinformatics annotation of the hypothetical proteins found by omics techniques can help to disclose additional virulence factors. Curr. Microbiol. 59, 451-456.
    • (2009) Curr. Microbiol. , vol.59 , pp. 451-456
    • Hernandez, S.1    Gomez, A.2    Cedano, J.3    Querol, E.4
  • 24
    • 55449125498 scopus 로고    scopus 로고
    • The rough guide to in silico function prediction, or how to use sequence and structure information to predict protein function
    • Punta, M., and, Ofran, Y., (2008) The rough guide to in silico function prediction, or how to use sequence and structure information to predict protein function. PLoS Comput. Biol. 4, e1000160.
    • (2008) PLoS Comput. Biol. , vol.4
    • Punta, M.1    Ofran, Y.2
  • 26
    • 77955670221 scopus 로고    scopus 로고
    • Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection
    • doi:310.1038/msb.2010.1043
    • Peña, M. I., Davlieva, M., Bennett, M. R., Olson, J. S., and, Shamoo, Y., (2010) Evolutionary fates within a microbial population highlight an essential role for protein folding during natural selection. Mol. Syst. Biol. 6, 387, doi:310.1038/msb.2010.1043.
    • (2010) Mol. Syst. Biol. , vol.6 , pp. 387
    • Peña, M.I.1    Davlieva, M.2    Bennett, M.R.3    Olson, J.S.4    Shamoo, Y.5
  • 27
    • 0028816953 scopus 로고
    • Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method
    • Geier, B. M., Schagger, H., Ortwein, C., Link, T. A., Hagen, W. R., Brandt, U., and Von Jagow, G,. (1995) Kinetic properties and ligand binding of the eleven-subunit cytochrome-c oxidase from Saccharomyces cerevisiae isolated with a novel large-scale purification method. Eur. J. Biochem. 227, 296-302.
    • (1995) Eur. J. Biochem. , vol.227 , pp. 296-302
    • Geier, B.M.1    Schagger, H.2    Ortwein, C.3    Link, T.A.4    Hagen, W.R.5    Brandt, U.6    Von Jagow, G.7
  • 28
    • 0023054139 scopus 로고
    • At least two nuclear gene products are specifically required for translation of a single yeast mitochondrial mRNA
    • Costanzo, M. C., Seaver, E. C., and, Fox, T. D., (1986) At least two nuclear gene products are specifically required for translation of a single yeast mitochondrial mRNA. EMBO J. 5, 3637-3641.
    • (1986) EMBO J. , vol.5 , pp. 3637-3641
    • Costanzo, M.C.1    Seaver, E.C.2    Fox, T.D.3
  • 29
    • 0024831985 scopus 로고
    • Disruption of the yeast nuclear PET54 gene blocks excision of mitochondrial intron aI5β from pre-mRNA for cytochrome c oxidase subunit I
    • Valencik, M. L., Kloeckener-Gruissem, B., Poyton, R. O., and, McEwen, J. E., (1989) Disruption of the yeast nuclear PET54 gene blocks excision of mitochondrial intron aI5 beta from pre-mRNA for cytochrome c oxidase subunit I. EMBO J. 8, 3899-3904. (Pubitemid 20016073)
    • (1989) EMBO Journal , vol.8 , Issue.12 , pp. 3899-3904
    • Valencik, M.L.1    Kloeckener-Gruissem, B.2    Poyton, R.O.3    McEwen, J.E.4
  • 30
    • 44349162917 scopus 로고    scopus 로고
    • A shared RNA-binding site in the Pet54 protein is required for translational activation and group I intron splicing in yeast mitochondria
    • DOI 10.1093/nar/gkn045
    • Kaspar, B. J., Bifano, A. L., and, Caprara, M. G., (2008) A shared RNA-binding site in the Pet54 protein is required for translational activation and group I intron splicing in yeast mitochondria. Nucleic Acids Res. 36, 2958-2968. (Pubitemid 351737188)
    • (2008) Nucleic Acids Research , vol.36 , Issue.9 , pp. 2958-2968
    • Kaspar, B.J.1    Bifano, A.L.2    Caprara, M.G.3
  • 32
    • 0037396292 scopus 로고    scopus 로고
    • Enzymes with extra talents: Moonlighting functions and catalytic promiscuity
    • DOI 10.1016/S1367-5931(03)00032-2
    • Copley, S. D., (2003) Enzymes with extra talents: moonlighting functions and catalytic promiscuity. Curr. Opin. Chem. Biol. 7, 265-272. (Pubitemid 36514958)
    • (2003) Current Opinion in Chemical Biology , vol.7 , Issue.2 , pp. 265-272
    • Copley, S.D.1
  • 33
    • 23944514504 scopus 로고    scopus 로고
    • Structural disorder throws new light on moonlighting
    • DOI 10.1016/j.tibs.2005.07.008, PII S0968000405002185
    • Tompa, P., Szasz, C., and, Buday, L., (2005) Structural disorder throws new light on moonlighting. Trends Biochem. Sci. 30, 484-489 (Pubitemid 41206503)
    • (2005) Trends in Biochemical Sciences , vol.30 , Issue.9 , pp. 484-489
    • Tompa, P.1    Szasz, C.2    Buday, L.3
  • 34
    • 14644435825 scopus 로고    scopus 로고
    • Intrinsically unstructured proteins and their functions
    • DOI 10.1038/nrm1589
    • Dyson, H. J., and, Wright, P. E., (2005) Intrinsically unstructured proteins and their functions. Nat. Rev. Mol. Cell. Biol. 2 6, 197-208. (Pubitemid 40314921)
    • (2005) Nature Reviews Molecular Cell Biology , vol.6 , Issue.3 , pp. 197-208
    • Dyson, H.J.1    Wright, P.E.2
  • 35
    • 25144472591 scopus 로고    scopus 로고
    • Showing your ID: Intrinsic disorder as an ID for recognition, regulation and cell signaling
    • DOI 10.1002/jmr.747
    • Uversky, V. N., Oldfield, C. J., and, Dunker, A. K., (2005) Showing your ID: intrinsic disorder as an ID for recognition, regulation and cell signaling. J. Mol. Recognit. 18, 343-384. (Pubitemid 41341287)
    • (2005) Journal of Molecular Recognition , vol.18 , Issue.5 , pp. 343-384
    • Uversky, V.N.1    Oldfield, C.J.2    Dunker, A.K.3
  • 36
    • 0004012131 scopus 로고
    • Chicago/London, The University of Chicago Press/Weidenfeld and Nicholson.
    • Lévi-Strauss, C., (1966). The Savage Mind. Chicago/London, The University of Chicago Press/Weidenfeld and Nicholson.
    • (1966) The Savage Mind
    • Lévi-Strauss, C.1
  • 37
    • 0242437856 scopus 로고    scopus 로고
    • The Gap1 general amino acid permease acts as an amino acid sensor for activation of protein kinase A targets in the yeast Saccharomyces cerevisiae
    • DOI 10.1046/j.1365-2958.2003.03732.x
    • Donaton, M. C., Holsbeeks, I., Lagatie, O., Van Zeebroeck, G., Crauwels, M., Winderickx, J., and, Thevelein, J. M., (2003) The Gap1 general amino acid permease acts as an amino acid sensor for activation of protein kinase A targets in the yeast Saccharomyces cerevisiae. Mol. Microbiol. 50, 911-929. (Pubitemid 37372253)
    • (2003) Molecular Microbiology , vol.50 , Issue.3 , pp. 911-929
    • Donaton, M.C.V.1    Holsbeeks, I.2    Lagatie, O.3    Van Zeebroeck, G.4    Crauwels, M.5    Winderickx, J.6    Thevelein, J.M.7
  • 38
    • 0032473497 scopus 로고    scopus 로고
    • The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae
    • DOI 10.1093/emboj/17.5.1236
    • Lorenz, M. C., and, Heitman, J., (1998) The MEP2 ammonium permease regulates pseudohyphal differentiation in Saccharomyces cerevisiae. EMBO J. 17, 1236-1247. (Pubitemid 28105503)
    • (1998) EMBO Journal , vol.17 , Issue.5 , pp. 1236-1247
    • Lorenz, M.C.1    Heitman, J.2
  • 39
    • 1942452749 scopus 로고    scopus 로고
    • Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae
    • DOI 10.1038/nature02424
    • Kellis, M., Birren, B. W., and, Lander, E. S., (2004) Proof and evolutionary analysis of ancient genome duplication in the yeast Saccharomyces cerevisiae. Nature 428, 617-624. (Pubitemid 38524797)
    • (2004) Nature , vol.428 , Issue.6983 , pp. 617-624
    • Kellis, M.1    Birren, B.W.2    Lander, E.S.3
  • 40
    • 0028865899 scopus 로고
    • Endocrine peptides 'moonlighting' as immune modulators: Roles for somatostatin and GH-releasing factor
    • Campbell, R. M., and, Scanes, C. G., (1995) Endocrine peptides 'moonlighting' as immune modulators: roles for somatostatin and GH-releasing factor. J. Endocrinol. 147, 383-396.
    • (1995) J. Endocrinol. , vol.147 , pp. 383-396
    • Campbell, R.M.1    Scanes, C.G.2


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