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Volumn 5, Issue 9, 2006, Pages 1490-1502

A eukaryote without catalase-containing microbodies: Neurospora crassa exhibits a unique cellular distribution of its four catalases

Author keywords

[No Author keywords available]

Indexed keywords

CATALASE; GREEN FLUORESCENT PROTEIN; HYBRID PROTEIN; HYDROGEN PEROXIDE; ISOENZYME; SIGNAL PEPTIDE;

EID: 33748856577     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00113-06     Document Type: Article
Times cited : (40)

References (55)
  • 1
  • 3
    • 0029787953 scopus 로고    scopus 로고
    • Identification of a yeast peroxisomal member of the family of AMP-binding proteins
    • Blobel, F., and R. Erdmann. 1996. Identification of a yeast peroxisomal member of the family of AMP-binding proteins. Eur. J. Biochem. 240:468-476.
    • (1996) Eur. J. Biochem. , vol.240 , pp. 468-476
    • Blobel, F.1    Erdmann, R.2
  • 4
    • 0022448483 scopus 로고
    • How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes)
    • Borst, P. 1986. How proteins get into microbodies (peroxisomes, glyoxysomes, glycosomes). Biochim. Biophys. Acta 866:179-203.
    • (1986) Biochim. Biophys. Acta , vol.866 , pp. 179-203
    • Borst, P.1
  • 5
    • 0027767502 scopus 로고
    • A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences
    • Brunelli, J. P., and M. L. Pall. 1993. A series of yeast shuttle vectors for expression of cDNAs and other DNA sequences. Yeast 9:1299-1308.
    • (1993) Yeast , vol.9 , pp. 1299-1308
    • Brunelli, J.P.1    Pall, M.L.2
  • 6
    • 0024550677 scopus 로고
    • Evidence for three differentially regulated catalase genes in Neurospora crassa: Effects of oxidative stress, heat shock, and development
    • Chary, P., and D. O. Natvig. 1989. Evidence for three differentially regulated catalase genes in Neurospora crassa: effects of oxidative stress, heat shock, and development. J. Bacteriol. 171:2646-2652.
    • (1989) J. Bacteriol. , vol.171 , pp. 2646-2652
    • Chary, P.1    Natvig, D.O.2
  • 8
    • 0018085738 scopus 로고
    • Regulation of catalase synthesis in Saccharomyces cerevisiae by carbon catabolite repression
    • Cross, H. S., and H. Ruis. 1978. Regulation of catalase synthesis in Saccharomyces cerevisiae by carbon catabolite repression. Mol. Gen. Genet. 166: 37-43.
    • (1978) Mol. Gen. Genet. , vol.166 , pp. 37-43
    • Cross, H.S.1    Ruis, H.2
  • 10
    • 0013897667 scopus 로고
    • Peroxisomes (microbodies and related particles)
    • de Duve, C., and P. Baudhuin. 1966. Peroxisomes (microbodies and related particles). Physiol. Rev. 46:323-357.
    • (1966) Physiol. Rev. , vol.46 , pp. 323-357
    • De Duve, C.1    Baudhuin, P.2
  • 11
    • 1842291916 scopus 로고
    • Isolation of peroxisome-deficient mutants of Saccharomyces cerevisiae
    • Erdmann, R., M. Veenhuis, D. Mertens, and W. H. Kunau. 1989. Isolation of peroxisome-deficient mutants of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 86:5419-5423.
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5419-5423
    • Erdmann, R.1    Veenhuis, M.2    Mertens, D.3    Kunau, W.H.4
  • 12
    • 0028962570 scopus 로고
    • Molecular cloning, sequencing and sequence analysis of the fox-2 gene of Neurospora crassa encoding the multifunctional beta-oxidation protein
    • Fossa, A., A. Beyer, E. Pfitzner, B. Wenzel, and W. H. Kunau. 1995. Molecular cloning, sequencing and sequence analysis of the fox-2 gene of Neurospora crassa encoding the multifunctional beta-oxidation protein. Mol. Gen. Genet. 247:95-104.
    • (1995) Mol. Gen. Genet. , vol.247 , pp. 95-104
    • Fossa, A.1    Beyer, A.2    Pfitzner, E.3    Wenzel, B.4    Kunau, W.H.5
  • 13
    • 4444362481 scopus 로고    scopus 로고
    • GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa
    • Freitag, M., P. C. Hickey, N. B. Raju, E. U. Selker, and N. D. Read. 2004. GFP as a tool to analyze the organization, dynamics and function of nuclei and microtubules in Neurospora crassa. Fungal Genet. Biol. 41:897-910.
    • (2004) Fungal Genet. Biol. , vol.41 , pp. 897-910
    • Freitag, M.1    Hickey, P.C.2    Raju, N.B.3    Selker, E.U.4    Read, N.D.5
  • 15
    • 0025760348 scopus 로고
    • The C-terminal domain of plant catalases. Implications for a glyoxysomal targeting sequence
    • Gonzalez, E. 1991. The C-terminal domain of plant catalases. Implications for a glyoxysomal targeting sequence. Eur. J. Biochem. 199:211-215.
    • (1991) Eur. J. Biochem. , vol.199 , pp. 211-215
    • Gonzalez, E.1
  • 18
    • 0034573311 scopus 로고    scopus 로고
    • Evolution of urate-degrading enzymes in animal peroxisomes
    • Hayashi, S., S. Fujiwara, and T. Noguchi. 2000. Evolution of urate-degrading enzymes in animal peroxisomes. Cell Biochem. Biophys. 32:123-129.
    • (2000) Cell Biochem. Biophys. , vol.32 , pp. 123-129
    • Hayashi, S.1    Fujiwara, S.2    Noguchi, T.3
  • 19
    • 18944372099 scopus 로고    scopus 로고
    • Biogenesis of peroxisomes. Topogenesis of the peroxisomal membrane and matrix proteins
    • Heiland, I., and R. Erdmann. 2005. Biogenesis of peroxisomes. Topogenesis of the peroxisomal membrane and matrix proteins. FEBS J. 272:2362-2372.
    • (2005) FEBS J. , vol.272 , pp. 2362-2372
    • Heiland, I.1    Erdmann, R.2
  • 20
    • 0018308739 scopus 로고
    • Catalase of Neurospora crassa. 1. Induction, purification, and physical properties
    • Jacob, G. S., and W. H. Orme-Johnson. 1979. Catalase of Neurospora crassa. 1. Induction, purification, and physical properties. Biochemistry 18:2967-2975.
    • (1979) Biochemistry , vol.18 , pp. 2967-2975
    • Jacob, G.S.1    Orme-Johnson, W.H.2
  • 21
    • 0033782946 scopus 로고    scopus 로고
    • A new self-assembled peroxisomal vesicle required for efficient resealing of the plasma membrane
    • Jedd, G., and N. H. Chua. 2000. A new self-assembled peroxisomal vesicle required for efficient resealing of the plasma membrane. Nat. Cell Biol. 2:226-231.
    • (2000) Nat. Cell Biol. , vol.2 , pp. 226-231
    • Jedd, G.1    Chua, N.H.2
  • 22
    • 0036231821 scopus 로고    scopus 로고
    • Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases
    • Johnson, C. H., M. G. Klotz, J. L. York, V. Kruft, and J. E. McEwen. 2002. Redundancy, phylogeny and differential expression of Histoplasma capsulatum catalases. Microbiology 148:1129-1142.
    • (2002) Microbiology , vol.148 , pp. 1129-1142
    • Johnson, C.H.1    Klotz, M.G.2    York, J.L.3    Kruft, V.4    McEwen, J.E.5
  • 23
    • 0035145679 scopus 로고    scopus 로고
    • Multiple catalase genes are differentially regulated in Aspergillus nidulans
    • Kawasaki, L., and J. Aguirre. 2001. Multiple catalase genes are differentially regulated in Aspergillus nidulans. J. Bacteriol. 183:1434-1440.
    • (2001) J. Bacteriol. , vol.183 , pp. 1434-1440
    • Kawasaki, L.1    Aguirre, J.2
  • 24
    • 0025787395 scopus 로고
    • Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes
    • Keller, G. A., S. Krisans, S. J. Gould, J. M. Sommer, C. C. Wang, W. Schliebs, W. Kunau, S. Brody, and S. Subramani. 1991. Evolutionary conservation of a microbody targeting signal that targets proteins to peroxisomes, glyoxysomes, and glycosomes. J. Cell Biol. 114:893-904.
    • (1991) J. Cell Biol. , vol.114 , pp. 893-904
    • Keller, G.A.1    Krisans, S.2    Gould, S.J.3    Sommer, J.M.4    Wang, C.C.5    Schliebs, W.6    Kunau, W.7    Brody, S.8    Subramani, S.9
  • 25
    • 0021990075 scopus 로고
    • Inducible β-oxidation pathway in Neurospora crassa
    • Kionka, C., and W. H. Kunau. 1985. Inducible β-oxidation pathway in Neurospora crassa. J. Bacteriol. 161:153-157.
    • (1985) J. Bacteriol. , vol.161 , pp. 153-157
    • Kionka, C.1    Kunau, W.H.2
  • 27
    • 0037067768 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p
    • Klein, A. T., M. van den Berg, G. Bottger, H. F. Tabak, and B. Distel. 2002. Saccharomyces cerevisiae acyl-CoA oxidase follows a novel, non-PTS1, import pathway into peroxisomes that is dependent on Pex5p. J. Biol. Chem. 277:25011-25019.
    • (2002) J. Biol. Chem. , vol.277 , pp. 25011-25019
    • Klein, A.T.1    Van Den Berg, M.2    Bottger, G.3    Tabak, H.F.4    Distel, B.5
  • 28
    • 0027507025 scopus 로고
    • Two independent peroxisomal targeting signals in catalase a of Saccharomyces cerevisiae
    • Kragler, F., A. Langeder, J. Raupachova, M. Binder, and A. Hartig. 1993. Two independent peroxisomal targeting signals in catalase A of Saccharomyces cerevisiae. J. Cell Biol. 120:665-673.
    • (1993) J. Cell Biol. , vol.120 , pp. 665-673
    • Kragler, F.1    Langeder, A.2    Raupachova, J.3    Binder, M.4    Hartig, A.5
  • 30
    • 0032509362 scopus 로고    scopus 로고
    • The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it
    • Lametschwandtner, G., C. Brocard, M. Fransen, P. Van Veldhoven, J. Berger, and A. Hartig. 1998. The difference in recognition of terminal tripeptides as peroxisomal targeting signal 1 between yeast and human is due to different affinities of their receptor Pex5p to the cognate signal and to residues adjacent to it. J. Biol. Chem. 273:33635-33643.
    • (1998) J. Biol. Chem. , vol.273 , pp. 33635-33643
    • Lametschwandtner, G.1    Brocard, C.2    Fransen, M.3    Van Veldhoven, P.4    Berger, J.5    Hartig, A.6
  • 31
    • 0014986891 scopus 로고
    • The origin and fate of microbodies in the fat body of an insect
    • Locke, M., and J. T. McMahon. 1971. The origin and fate of microbodies in the fat body of an insect. J. Cell Biol. 48:61-78.
    • (1971) J. Cell Biol. , vol.48 , pp. 61-78
    • Locke, M.1    McMahon, J.T.2
  • 32
    • 9644294511 scopus 로고    scopus 로고
    • Mitochondrial β-oxidation in Aspergillus nidulans
    • Maggio-Hall, L. A., and N. P. Keller. 2004. Mitochondrial β-oxidation in Aspergillus nidulans. Mol. Microbiol. 54:1173-1185.
    • (2004) Mol. Microbiol. , vol.54 , pp. 1173-1185
    • Maggio-Hall, L.A.1    Keller, N.P.2
  • 34
    • 0043234237 scopus 로고    scopus 로고
    • Asexual development is increased in Neurospora crassa cat-3-null mutant strains
    • Michan, S., F. Lledias, and W. Hansberg. 2003. Asexual development is increased in Neurospora crassa cat-3-null mutant strains. Eukaryot. Cell 2:798-808.
    • (2003) Eukaryot. Cell , vol.2 , pp. 798-808
    • Michan, S.1    Lledias, F.2    Hansberg, W.3
  • 36
    • 0023250363 scopus 로고
    • Induction and de novo synthesis of uricase, a nitrogen-regulated enzyme in Neurospora crassa
    • Nahm, B. H., and G. A. Marzluf. 1987. Induction and de novo synthesis of uricase, a nitrogen-regulated enzyme in Neurospora crassa. J. Bacteriol. 169: 1943-1948.
    • (1987) J. Bacteriol. , vol.169 , pp. 1943-1948
    • Nahm, B.H.1    Marzluf, G.A.2
  • 37
    • 0036249868 scopus 로고    scopus 로고
    • Neurospora crassa catalases, singlet oxygen and cell differentiation
    • Peraza, L., and W. Hansberg. 2002. Neurospora crassa catalases, singlet oxygen and cell differentiation. Biol. Chem. 383:569-575.
    • (2002) Biol. Chem. , vol.383 , pp. 569-575
    • Peraza, L.1    Hansberg, W.2
  • 38
    • 0029849741 scopus 로고    scopus 로고
    • Targeting of human catalase to peroxisomes is dependent upon a novel COOH-terminal peroxisomal targeting sequence
    • Purdue, P. E., and P. B. Lazarow. 1996. Targeting of human catalase to peroxisomes is dependent upon a novel COOH-terminal peroxisomal targeting sequence. J. Cell Biol. 134:849-862.
    • (1996) J. Cell Biol. , vol.134 , pp. 849-862
    • Purdue, P.E.1    Lazarow, P.B.2
  • 39
    • 0016669407 scopus 로고
    • Cytochemical discrimination between catalases and peroxidases using diaminobenzidine
    • Roels, F., E. Wisse, B. De Prest, and J. van der Meulen. 1975. Cytochemical discrimination between catalases and peroxidases using diaminobenzidine. Histochemistry 41:281-312.
    • (1975) Histochemistry , vol.41 , pp. 281-312
    • Roels, F.1    Wisse, E.2    De Prest, B.3    Van Der Meulen, J.4
  • 40
    • 0029937512 scopus 로고    scopus 로고
    • Pip2p: A transcriptional regulator of peroxisome proliferation in the yeast Saccharomyces cerevisiae
    • Rottensteiner, H., A. J. Kal, M. Filipits, M. Binder, B. Hamilton, H. F. Tabak, and H. Ruis. 1996. Pip2p: a transcriptional regulator of peroxisome proliferation in the yeast Saccharomyces cerevisiae. EMBO J. 15:2924-2934.
    • (1996) EMBO J. , vol.15 , pp. 2924-2934
    • Rottensteiner, H.1    Kal, A.J.2    Filipits, M.3    Binder, M.4    Hamilton, B.5    Tabak, H.F.6    Ruis, H.7
  • 41
    • 3042724871 scopus 로고    scopus 로고
    • Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals
    • Rottensteiner, H., A. Kramer, S. Lorenzen, K. Stein, C. Landgraf, R. Volkmer-Engert, and R. Erdmann. 2004. Peroxisomal membrane proteins contain common Pex19p-binding sites that are an integral part of their targeting signals. Mol. Biol. Cell 15:3406-3417.
    • (2004) Mol. Biol. Cell , vol.15 , pp. 3406-3417
    • Rottensteiner, H.1    Kramer, A.2    Lorenzen, S.3    Stein, K.4    Landgraf, C.5    Volkmer-Engert, R.6    Erdmann, R.7
  • 42
    • 0141541655 scopus 로고    scopus 로고
    • Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis
    • Rottensteiner, H., K. Stein, E. Sonnenhol, and R. Erdmann. 2003. Conserved function of Pex11p and the novel Pex25p and Pex27p in peroxisome biogenesis. Mol. Biol. Cell 14:4316-4328.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 4316-4328
    • Rottensteiner, H.1    Stein, K.2    Sonnenhol, E.3    Erdmann, R.4
  • 44
    • 4744375324 scopus 로고    scopus 로고
    • Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p
    • Schäfer, A., D. Kerssen, M. Veenhuis, W.-H. Kunau, and W. Schliebs. 2004. Functional similarity between the peroxisomal PTS2 receptor binding protein Pex18p and the N-terminal half of the PTS1 receptor Pex5p. Mol. Cell. Biol. 24:8895-8906.
    • (2004) Mol. Cell. Biol. , vol.24 , pp. 8895-8906
    • Schäfer, A.1    Kerssen, D.2    Veenhuis, M.3    Kunau, W.-H.4    Schliebs, W.5
  • 45
    • 17644393919 scopus 로고    scopus 로고
    • Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei
    • Schlecker, T., A. Schmidt, N. Dirdjaja, F. Voncken, C. Clayton, and R. L. Krauth-Siegel. 2005. Substrate specificity, localization, and essential role of the glutathione peroxidase-type tryparedoxin peroxidases in Trypanosoma brucei. J. Biol. Chem. 280:14385-14394.
    • (2005) J. Biol. Chem. , vol.280 , pp. 14385-14394
    • Schlecker, T.1    Schmidt, A.2    Dirdjaja, N.3    Voncken, F.4    Clayton, C.5    Krauth-Siegel, R.L.6
  • 46
    • 0019960467 scopus 로고
    • Regulation of L-amino acid oxidase and of D-amino acid oxidase in Neurospora crassa
    • Sikora, L., and G. A. Marzluf. 1982. Regulation of L-amino acid oxidase and of D-amino acid oxidase in Neurospora crassa. Mol. Gen. Genet. 186:33-39.
    • (1982) Mol. Gen. Genet. , vol.186 , pp. 33-39
    • Sikora, L.1    Marzluf, G.A.2
  • 47
    • 0036337231 scopus 로고    scopus 로고
    • Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: Implications for the first steps in PTS2 protein import
    • Stein, K., A. Schell-Steven, R. Erdmann, and H. Rottensteiner. 2002. Interactions of Pex7p and Pex18p/Pex21p with the peroxisomal docking machinery: implications for the first steps in PTS2 protein import. Mol. Cell. Biol. 22:6056-6069.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6056-6069
    • Stein, K.1    Schell-Steven, A.2    Erdmann, R.3    Rottensteiner, H.4
  • 48
    • 0033787313 scopus 로고    scopus 로고
    • Import of peroxisomal matrix and membrane proteins
    • Subramani, S., A. Koller, and W. B. Snyder. 2000. Import of peroxisomal matrix and membrane proteins. Annu. Rev. Biochem. 69:399-418.
    • (2000) Annu. Rev. Biochem. , vol.69 , pp. 399-418
    • Subramani, S.1    Koller, A.2    Snyder, W.B.3
  • 49
    • 0034466108 scopus 로고    scopus 로고
    • Hex-1, a gene unique to filamentous fungi, encodes the major protein of the Woronin body and functions as a plug for septal pores
    • Tenney, K., I. Hunt, J. Sweigard, J. I. Pounder, C. McClain, E. J. Bowman, and B. J. Bowman. 2000. Hex-1, a gene unique to filamentous fungi, encodes the major protein of the Woronin body and functions as a plug for septal pores. Fungal Genet. Biol. 31:205-217.
    • (2000) Fungal Genet. Biol. , vol.31 , pp. 205-217
    • Tenney, K.1    Hunt, I.2    Sweigard, J.3    Pounder, J.I.4    McClain, C.5    Bowman, E.J.6    Bowman, B.J.7
  • 50
    • 0025879292 scopus 로고
    • The β-oxidation system in catalase-free microbodies of the filamentous fungus Neurospora crassa. Purification of a multifunctional protein possessing 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-hydroxyacyl-CoA epimerase activities
    • Thieringer, R., and W. H. Kunau. 1991. The β-oxidation system in catalase-free microbodies of the filamentous fungus Neurospora crassa. Purification of a multifunctional protein possessing 2-enoyl-CoA hydratase, L-3-hydroxyacyl-CoA dehydrogenase, and 3-hydroxyacyl-CoA epimerase activities. J. Biol. Chem. 266:13110-13117.
    • (1991) J. Biol. Chem. , vol.266 , pp. 13110-13117
    • Thieringer, R.1    Kunau, W.H.2
  • 51
    • 10544224537 scopus 로고    scopus 로고
    • Induction of β-oxidation enzymes and microbody proliferation in Aspergillus nidulans
    • Valenciano, S., J. R. Lucas, A. Pedregosa, I. F. Monistrol, and F. Laborda. 1996. Induction of β-oxidation enzymes and microbody proliferation in Aspergillus nidulans. Arch. Microbiol. 166:336-341.
    • (1996) Arch. Microbiol. , vol.166 , pp. 336-341
    • Valenciano, S.1    Lucas, J.R.2    Pedregosa, A.3    Monistrol, I.F.4    Laborda, F.5
  • 52
    • 0017152869 scopus 로고
    • Cytochemical studies on the localization of methanol oxidase and other oxidases in peroxisomes of methanol-grown Hansenula polymorpha
    • Veenhuis, M., J. P. van Dijken, and W. Harder. 1976. Cytochemical studies on the localization of methanol oxidase and other oxidases in peroxisomes of methanol-grown Hansenula polymorpha. Arch. Microbiol. 111:123-135.
    • (1976) Arch. Microbiol. , vol.111 , pp. 123-135
    • Veenhuis, M.1    Van Dijken, J.P.2    Harder, W.3
  • 53
    • 0020017929 scopus 로고
    • Two types of microbodies in Neurospora crassa
    • Wanner, G., and R. R. Theimer. 1982. Two types of microbodies in Neurospora crassa. Ann. N. Y. Acad. Sci. 386:269-284.
    • (1982) Ann. N. Y. Acad. Sci. , vol.386 , pp. 269-284
    • Wanner, G.1    Theimer, R.R.2
  • 54
    • 0028061714 scopus 로고
    • The Hansenula polymorpha PER1 gene is essential for peroxisome biogenesis and encodes a peroxisomal matrix protein with both carboxy- And amino-terminal targeting signals
    • Waterham, H. R., V. I. Titorenko, P. Haima, J. M. Cregg, W. Harder, and M. Veenhuis. 1994. The Hansenula polymorpha PER1 gene is essential for peroxisome biogenesis and encodes a peroxisomal matrix protein with both carboxy- and amino-terminal targeting signals. J. Cell Biol. 127:737-749.
    • (1994) J. Cell Biol. , vol.127 , pp. 737-749
    • Waterham, H.R.1    Titorenko, V.I.2    Haima, P.3    Cregg, J.M.4    Harder, W.5    Veenhuis, M.6
  • 55
    • 0015152970 scopus 로고
    • An improved procedure using ferricyanide for detecting catalase isozymes
    • Woodbury, W., A. K. Spencer, and M. A. Stahman. 1971. An improved procedure using ferricyanide for detecting catalase isozymes. Anal. Biochem. 44:301-305.
    • (1971) Anal. Biochem. , vol.44 , pp. 301-305
    • Woodbury, W.1    Spencer, A.K.2    Stahman, M.A.3


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