Human PEX7 encodes the peroxisomal PTS2 receptor and is responsible for rhizomelic chondrodysplasia punctata

Nature Genetics

Volumn 15, Issue 4, 1997, Pages 369-376

  Braverman, Nancy ^a   Steel, Gary ^a   Obie, Cassandra ^a   Moser, Ann ^a   Moser, Hugo ^a   Gould, Stephen J ^a   Valle, David ^a  

^a JOHNS HOPKINS UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CELL PROTEIN; DIHYDROXYACETONE PHOSPHATE ACYLTRANSFERASE; PEROXISOME PROTEIN; PHYTANIC ACID; PLASMALOGEN; RNA; SYNTHETASE; UNCLASSIFIED DRUG; VERY LONG CHAIN FATTY ACID;

AMINO ACID SEQUENCE; ARTICLE; CELLULAR DISTRIBUTION; CHONDRODYSPLASIA PUNCTATA; CHROMOSOME 6; CHROMOSOME MAP; CONTROLLED STUDY; GENE MUTATION; HUMAN; HUMAN CELL; HUMAN TISSUE; MOUSE; NONHUMAN; OPEN READING FRAME; PEROXISOME; PRIORITY JOURNAL; PROTEIN LOCALIZATION; PROTEIN SECONDARY STRUCTURE; SEQUENCE HOMOLOGY; SKIN FIBROBLAST;

AMINO ACID SEQUENCE; ANIMALS; CELLS, CULTURED; CHONDRODYSPLASIA PUNCTATA, RHIZOMELIC; CHROMOSOME MAPPING; CHROMOSOMES, HUMAN, PAIR 6; DNA, COMPLEMENTARY; FIBROBLASTS; GENE EXPRESSION; GENES; HUMANS; MICE; MOLECULAR SEQUENCE DATA; MUTATION; ORGAN SPECIFICITY; RECEPTORS, CYTOPLASMIC AND NUCLEAR; RECOMBINANT FUSION PROTEINS; RNA, MESSENGER; SEQUENCE HOMOLOGY, AMINO ACID;

MURINAE;

EID: 0030946632     PISSN: 10614036     EISSN: None     Source Type: Journal    
DOI: 10.1038/ng0497-369     Document Type: Article

References (69)

1. Brul, S. et al. Genetic hetrogeneity in the cerebrohepatorenal (Zellweger) syndrome and other inherited disorders with a generalized impairment of peroxisomal functions - A study using complementation analysis. J. Clin. Invest. 81, 1710-1715 (1988).
2. Shimozawa, N. et al. Standardization of complementation grouping of peroxisome-deficient disorders and the second Zellweger patient with peroxisomal assembly factor-I (PAF-I) defect. Am. J. Hum. Genet. 52, 843-844 (1993).
3. Moser, A.B. et al. Phenotype of patients with peroxisomal disorders subdivided into sixteen complementation groups. J. Pediatr. 127, 13-22 (1995).
4. Poulos, A. et al. Peroxisomal assembly defects: Clinical, pathologic and biochemical findings in two patients in a newly identified complementation group. J. Pediatr. 127, 596-599 (1995).
5. Lazarow, P.B. & Moser, H.W. in The Metabolic and Molecular Bases of Inherited Disease. (eds Scriver, C.R. et al.) 2287-2324 (McGraw-Hill, New York, 1995).
6. Slawecki, M. et al. Identification of three distinct peroxisomal protein import defects in patients with peroxisome biogenesis disorders. J. Cell Sci. 108, 1817-1829 (1995).
7. Hoefler, G. et al. Biochemical abnormalities in rhizomelic chondrodysplasia punctata. J. Pediatr. 112, 726-733 (1988).
8. Heikoop, J.C. et al. Rhizomelic chondrodysplasia punctata: Deficiency of 3-oxoacyl-coenzyme A thiolase in peroxisomes and impaired processing of the enzyme. J. Clin. Invest. 86, 126-130 (1990).
9. Poll-The, B.T. et al. A new type of chondrodysplasia punctata associated with peroxisomal dysfunction. J. Inher. Metab. Dis. 14, 361-363 (1991).
10. Gray, R.G.F. et al. Rhizomelic chondrodysplasia punctata - a new clinical variant. J. Inher. Metab. Dis. 15, 931-932 (1992).
11. Nuoffer, J.M. et al. Chondrodysplasia punctata with a mild clinical course. J. Inher. Metab. Dis. 17, 60-66 (1994).
12. Barth, P.G., Wanders, R.J.A., Schutgens, R.B.H. & Staalman, C.R. Variant rhizomelic chondrodysplasia punctata (RCDP) with normal plasma phytanic acid: Clinico-biochemical delineation of a subtype and complementation studies. Am. J. Med. Genet. 62, 164-168 (1996).
13. Smeitink, J.A.M. et al. Bone dysplasia associated with phytanic acid accumulation and deficient plasmalogen synthesis: A peroxisomal entity amenable to plasmapheresis. J. Inher. Metab. Dis. 15, 377-380 (1992).
14. Pike, M.G. et al. Congenital rubella syndrome associated with calcific epiphyseal stippling and peroxisomal dysfunction. J. Pediatr 116, 88-94 (1990).
15. Motley, A.M. et al. Non-rhizomelic and rhizomelic chondrodysplasia punctata within a single complementation group. Biochim. Biophys. Acta. 1315, 153-158 (1996).
16. Wanders, R.J.A., Schumacher, H., Heikoop, J., Schutgens, R.B.H. & Tager, J.M. Human dihydroxyacetonephosphate acyltransferase deficiency: A new peroxisomal disorder. J. Inher. Metab. Dis. 15, 389-391 (1992).
17. Wanders, R.J.A. et al. Human alkyldihydroxyacetonephosphate synthase deficiency: A new peroxisomal disorder. J. Inher. Metab. Dis. 17, 315-318 (1994).
18. Distel, B. et al. A unified nomenclature for peroxisome biogenesis factors. J. Cell Biol. 135, 1-3 (1996).
19. Kunau, W.H. et al. Two complementary approaches to study peroxisome biogenesis in Saccharomyces cerevisiae: Forward and reversed genetics. Biochimie 75, 209-224 (1993).
20. Gould, S.J., McCollum, D., Spong, A.P., Heyman, J.A. & Subramani, S. Development of the yeast Pichia pastoris as a model organism for a genetic and molecular analysis of peroxisome assembly. Yeast 8, 613-628 (1992).
21. Purdue, P.E. & Lazarow, P.B. Peroxisomal biogenesis: Multiple pathways of protein import. J. Biol. Chem. 269, 30065-30068 (1994).
22. Rachubinski, R.A., Subramani, S. How proteins penetrate peroxisomes. Cell 83, 525-528 (1995).
23. Gould, S.J., Keller, G.A., Hosken, N., Wilkinson, J. & Subramani, S. A conserved tripeptide sorts proteins to peroxisomes. J. Cell Biol. 108, 1657-1664 (1989).
24. Subramani, S. Protein import into peroxisomes and biogenesis of the organelle. Annu. Rev. Cell. Biol. 9, 445-478 (1993).
25. Gietl, C., Faber, K.N., van der Klei, I.J. & Veenhuis, M. Mutational analysis of the N-terminal topogenic signal of watermelon glyoxysomal malate dehydrogenase using the heterologous host Hansenula polymorpha. Proc. Natl. Acad. Sci. USA 91, 3151-3155 (1994).
26. Swinkels, B.W., Gould, S.J., Bodnar, A.G., Rachubinski, R.A. & Subramani, S. A novel, cleavable peroxisomal targeting signal at the amino-terminus of the rat 3-ketoacyl-CoA thiolase. EMBO J. 10, 3255-3262 (1991).
27. Osumi, T. et al. Amino-terminal presequence of the precursor of peroxisomal 3-ketoacyl-CoA thiolase is a cleavable signal peptide for peroxisomal targeting. Biochem. Biophys. Res. Comm. 181, 947-954 (1991).
28. Faber, K.N. et al. The N-terminus of amine oxidase of Hansenula polymorpha contains a peroxisomal targeting signal. FEBS Lett. 357, 115-120 (1995).
29. Shimozawa, N. et al. A human gene responsible for Zellweger syndrome that affects peroxisome assembly. Science 255, 1132-1134 (1992).
30. Dodt, G. et al. Mutations in the PTS1 receptor gene, PXR1, define complementation group 2 of the peroxisome biogenesis disorders. Nature Genet. 9, 115-124 (1995).
31. Wiemer, E.A.C. et al. Human peroxisomal targeting signal-1 receptor restores peroxisomal protein import in cells from patients with fatal peroxisomal disorders. J. Cell Biol. 130, 51-65 (1995).
32. Fransen, M. et al. Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor. J. Biol. Chem. 270, 7731-7736 (1995).
33. Marynen, P., Fransen, M., Raeymaekers, P., Mannaerts, G.P. & Van Veldhoven, P.P. The gene for the peroxisomal targeting signal import receptor (PXR1) is located on human chromosome 12p13, flanked by TPI1 and D12S1089. Genomics 30, 366-368 (1995).
34. Yahraus, T. et al. The peroxisome biogenesis disorder group 4 gene, PXAAA1, encodes a cytoplasmic ATPase required for stability of the PTS1 receptor. EMBO J. 15, 2914-2923 (1996).
35. Fukuda, S. et al. Human peroxisome assembly factor-2 (PAF-2): A gene responsible for Group C peroxisome biogenesis disorder in humans. Am. J. Hum. Genet. 59, 1210-1220 (1996).
36. Gould, S.J. et al. Pex13p is an SH3 protein of the peroxisome membrane and a docking factor for the predominantly cytoplasmic PTS1 receptor. J. Cell Biol. 135, 85-95 (1996).
37. Elgersma, Y. et al. The SH3 domain of the Saccharomyces cerevisiae peroxisomal membrane protein Pex13p functions as a docking site for Pex5p, a mobile receptor for the import of PT1-containing proteins. J. Cell Biol. 135, 97-109 (1996).
38. Erdmann, R. & Blobel, G. Identification of Pex13p, a peroxisomal membrane receptor for the PTS1 recognition factor. J. Cell Biol. 135, 111-121 (1996).
39. Marzioch, M., Erdmann, R., Veenhuis, M. & Kunau, W.H. PAS7 encodes a novel yeast member of the WD-40 protein family essential for import of 3-oxoacyl-CoA thiolase, a PTS2-containing protein, into peroxisomes. EMBO J. 13, 4908-4918 (1994).
40. Zhang, J.W. & Lazarow, P.B. PEB1 (PAS7) in Saccharomyces cerevisiae encodes a hydrophilic, intra-peroxisomal protein that is a member of the WD repeat family and is essential for the import of thiolase into peroxisomes. J. Cell Biol. 129, 65-80 (1995).
41. Heikoop, J.C. et al. Peroxisomes of normal morphology but deficient in 3-oxoacyl-CoA thiolase in rhizomelic chondrodysplasia punctata fibroblasts. Biochim. Biophys. Acta. 1097, 69-77 (1991).
42. Renting, P. et al. The import receptor for the peroxisomal targeting signal 2 (PTS2) in Saccharomyces cerevisiae is encoded by the PAS7 gene. EMBO J. 15, 2901-2913 (1996).
43. 2-terminal peptide. J. Cell. Biol. 132, 325-334 (1996).
44. Motley, A., Hettema, E., Distel, B. & Tabak, H. Differential protein import deficiencies in human peroxisome assembly disorders. J. Cell. Biol. 125, 755-767 (1994).
45. Dodt, G., Braverman, N., Valle, D. & Gould, S.J. From expressed sequence tags to peroxisome biogenesis disorder genes. New York Acad. Sci. (in the press).
46. Hieter, P., Bassett, D.E. & Valle, D. The yeast genome - a common biological currency. Nature Genet. 13, 253-255 (1996).
47. Altschul, S.F., Gish, W., Miller, W., Myers, E.W. & Lipman, D.J. Basic local alignment search tool. J. Mol. Biol. 215, 403-410 (1990).
48. Kozak, M. Regulation of translation in eukaryotic systems. Annu. Rev. Cell Biol. 8, 197-225 (1992).
49. van der Voorn, L. & Ploegh, H. The WD-40 repeat. FEBS Letts. 307, 131-134 (1992).
50. Neer, E.J., Schmidt, C.J., Nambudripad, R. & Smith, T.F. The ancient regulatory-protein family of WD-repeat proteins. Nature 371, 297-300 (1994).
51. γ2. Cell 83, 1047-1058 (1995).
52. Adams-Klages, S. et al. FAN, a novel WD-repeat protein, couples the p55 TNF-receptor to neutral sphingomyelinase. Cell 86, 937-947 (1996).
53. Henning, K.A. et al. The Cockayne syndrome group A gene encodes a WD repeat protein that interacts with CSB protein and a subunit of RNA polymerase II TFIIH. Cell 82, 555-564 (1995).
54. Fong, H.K.W. et al. Repetitive segmental structure of the transducin β subunit: Homology with the CDC4 gene and identification of related mRNAs. Proc. Natl. Acad. Sci. USA 83, 2162-2166 (1986).
55. Goebl, M. & Yanagida, M. The TPR snap helix: a novel protein repeat motif from mitosis to transcription. TIBS 16, 173-177 (1991).
56. Tzamarias, D. & Struhl, K. Functional dissection of the yeast Cyc8-Tup1 transcriptional co-repressor complex. Nature 369, 758-761 (1994).
57. Brody, L.C. et al. Ornithine-δ-aminotransferase mutations causing gyrate atrophy: Allelic heterogeneity and functional consequences. J. Biol. Chem. 267, 3302-3307 (1992).
58. Dietz, H.C. et al. The skipping of constitutive exons in vivo induced by nonsense mutations. Science 259, 680-683 (1993).
59. Maquat, L.E. When cells stop making sense: Effects of nonsense codons on RNA metabolism in vertebrate cells. RNA 1, 453-465 (1995).
60. Cooper, D.N., Krawszak, M. & Antonarakis, S.E. in The Metabolic and Molecular Bases of Inherited Disease, (eds Scriver, C.R. et al.) 259-291 (McGraw Hill, New York, 1995).
61. Feinberg, A.P & Vogelstein, B. A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal. Biochem. 132, 6-13 (1983).
62. Engelhardt, J.F., Steel, G. & Valle, D. Transcriptional analysis of the human ornithine aminotransferase promoter. J. Biol. Chem. 266, 752-758 (1991).
63. Sambrook, J., Fritsch, E.F. & Maniatis, T. Molecular Cloning: A Laboratory Manual, Cold Spring Harbor Laboratory Press, Cold Spring Harbor, (1989).
64. Chirgwin, J.M., Przybyla, A.E., MacDonald, R.J. & Rutter, W.J. Isolation of biologically active ribonucleic acid from sources enriched in ribonuclease. Biochem. 18, 5294-5299 (1979).
65. Mitchell, G.A. et al. Human ornithine-δ-aminotransferase: cDNA cloning and analysis of the structural gene. J. Biol. Chem. 263, 14288-14295 (1988).
66. Gärtner, J., Moser, H. & Valle, D. Mutations in the 70 kD peroxisomal membrane protein gene in Zellweger syndrome. Nature Genet. 1, 16-23 (1992).
67. Innis, M.A., Gelfand, D.H., Sninsky, J.J. & White, T.J. PCR Protocols: A Guide to Methods and Applications. (Academic Press, New York, 1990).
68. Evan, G.I., Lewis, G.K., Ramsay, G. & Bishop, J.M. Isolation of monoclonal antibodies specific for human c-myc proto-oncogene product. Mol. Cell Biol. 5, 3610-3616 (1985).
69. Gould, S.J., Keller, G.A. & Subramani, S. Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase. J. Cell Biol. 105, 2923-2931 (1987).