The Hansenula polymorpha peroxisomal targeting signal 1 receptor, Pex5p, functions as a tetramer

FEBS Letters

Volumn 581, Issue 9, 2007, Pages 1758-1762

  Moscicka, Katarzyna B ^a   Klompmaker, Sandra H ^a   Wang, Dongyuan ^a   van der Klei, Ida J ^a   Boekema, Egbert J ^a  

^a UNIVERSITY OF GRONINGEN   (Netherlands)

Author keywords

Electron microscopy; Hansenula polymorpha; Membrane transport; Peroxisome; Pex5p

Indexed keywords

CATALASE; MATRIX PROTEIN; PEROXIN; PEROXISOMAL TARGETING SIGNAL 1 RECEPTOR; PEROXISOMAL TARGETING SIGNAL 20 RECEPTOR; TETRAMER; UNCLASSIFIED DRUG;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; HANSENULA POLYMORPHA; NONHUMAN; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN CONFORMATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN PURIFICATION; PROTEIN STRUCTURE; STRUCTURE ANALYSIS;

DIMERIZATION; FUNGAL PROTEINS; MODELS, MOLECULAR; MULTIPROTEIN COMPLEXES; PICHIA; PROTEIN BINDING; RECEPTORS, CYTOPLASMIC AND NUCLEAR;

PICHIA ANGUSTA;

EID: 34247132205     PISSN: 00145793     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.febslet.2007.03.061     Document Type: Article

References (20)

1. Gatto G.J., Geisbrecht B.V., Gould S.J., and Berg J.M. Peroxisomal targeting signal-1 recognition by the TPR domains of human PEX5. Nat. Struct. Biol. 7 12 (2000) 1091-1095
2. Gatto G.J., Maynard E.L., Guerrerio A.L., Geisbrecht B.V., Gould S.J., and Berg J.M. Correlating structure and affinity for PEX5:PTS1 complexes. Biochemistry 42 6 (2003) 1660-1666
3. Stanley W.A., Filipp F.V., Kursula P., Schuller N., Erdmann R., Schliebs W., Sattler M., and Wilmanns M. Recognition of a functional peroxisome type 1 target by the dynamic import receptor pex5p. Mol. Cell. 24 5 (2006) 653-663
4. Schliebs W., Saidowsky J., Agianian B., Dodt G., Herberg F.W., and Kunau W.H. Recombinant human peroxisomal targeting signal receptor PEX5. J. Biol. Chem. 274 9 (1999) 5666-5673
5. Boteva R., Koek A., Visser N.V., Visser A.J., Krieger E., Zlateva T., Veenhuis M., and Van der Klei I.J. Fluorescence analysis of the Hansenula polymorpha peroxisomal targeting signal-1 receptor, Pex5p. Eur. J. Biochem. 270 21 (2003) 4332-4338
6. Wang D., Visser N.V., Veenhuis M., and van der Klei I.J. Physical interactions of the peroxisomal targeting signal 1 receptor Pex5p, studied by fluorescence correlations spectroscopy. J. Biol. Chem. 278 44 (2003) 43340-43345
7. Costa-Rodrigues J., Carvalho A.F., Fransen M., Hambruch E., Schliebs W., Sa-Miranda C., and Azevedo J.E. Pex5p, the peroxisomal cycling receptor, is a monomeric non-globular protein. J. Biol. Chem. 280 26 (2005) 24404-24411
8. Carvalho A.F., Costa-Rodrigues J., Correia I., Costa Pessoa J., Faria T.Q., Martins C.L., Fransen M., Sa-Miranda C., and Azevedo J.E. The N-terminal half of the peroxisomal cycling receptor Pex5p is a natively unfolded domain. J. Mol. Biol. 356 4 (2006) 864-875
9. Kiel J.A., Veenhuis M., and van der Klei I.J. PEX genes in fungal genomes: common, rare or redundant. Traffic 7 10 (2006) 1291-1303
10. Leon S., Zhang L., McDonald W.H., Yates J., Cregg J.M., and Subramani S. Dynamics of the peroxisomal import cycle of PpPex20p: ubiquitin-dependent localization and regulation. J. Cell Biol. 172 1 (2006) 67-78
11. Otzen M., Wang D., Lunenborg M.G.J., and van der Klei I.J. Hansenula polymorpha Pex20p is an oligomer that binds the peroxisomal targeting signal 2 (PTS2). J. Cell. Sci. 118 15 (2005) 3409-3418
12. Frank J. Single-particle imaging of macromolecules by cryoelectron microscopy. Annu. Rev. Biophys. Biomol. Struct. 31 (2002) 309-319
13. Van Heel M., Gowen B., Matadeen R., Orlova E.V., Finn R., Pape T., Cohen D., Stark H., Schmidt R., Schatz M., and Patwardhan A. Single-particle electron cryo-microscopy: towards atomic resolution. Quat. Rev. Biophys. 33 4 (2000) 307-369
14. Penczek P., Radermacher M., and Frank J. Three dimensional reconstruction of single particles embedded in ice. Ultramicroscope 40 1 (1992) 33-53
15. van Heel M. Similarity measures between images. Ultramicroscope 21 1 (1987) 95-100
16. Koek, A. (2006) Peroxisomes in Hansenula polymorpha. Ph.D. Thesis University of Groningen, The Netherlands.
17. Abrahams J.P., Leslie A.G.W., Lutter R., and Walker J.E. Structure at 2.8-Angstrom resolution of F1-ATPase from bovine heart-mitochondria. Nature 370 6491 (1994) 621-628
18. Leon S., Goodman J.M., and Subramani S. Uniqueness of the mechanism of protein import into the peroxisome matrix: transport of folded, co-factor-bound and oligomeric proteins by shuttling receptors. Biochim. Biophys. Acta 1762 12 (2006) 1552-1564
19. Oates J., Mathers J., Mangels D., Kühlbrandt W., Robinson C., and Model K. Consensus structural features of purified bacterial TatABC complexes. J. Mol. Biol. 330 2 (2003) 277-286
20. Sugadev, R., Balasundaresan, D., Ponnuswamy, M.N., Kumaran, D., Swaminathan, S., Sekar, K. The crystal structure of bovine liver catalase. Unpublished, PDB entry: 1TGU.