Changes in Targeting Efficiencies of Proteins to Plant Microbodies Caused by Amino Acid Substitutions in the Carboxy-terminal Tripeptide

Plant and Cell Physiology

Volumn 38, Issue 6, 1997, Pages 759-768

  Hayashi, Makoto ^a   Aoki, Masahiro ^a   Kondo, Maki ^a   Nishimura, Mikio ^a  

^a NATIONAL INSTITUTE FOR BASIC BIOLOGY   (Japan)

Author keywords

Arabidopsis thaliana; Glyoxysome; Leaf peroxisome; Microbody; Protein sorting; Targeting signal

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA; EMBRYOPHYTA;

AMINO ACID; SIGNAL PEPTIDE; VEGETABLE PROTEIN;

ARABIDOPSIS; ARTICLE; CHEMISTRY; IMMUNOELECTRON MICROSCOPY; METABOLISM; MICROBODY; TRANSGENIC PLANT; ULTRASTRUCTURE;

AMINO ACIDS; ARABIDOPSIS; MICROBODIES; MICROSCOPY, IMMUNOELECTRON; PLANT PROTEINS; PLANTS, GENETICALLY MODIFIED; PROTEIN SORTING SIGNALS;

EID: 0031154927     PISSN: 00320781     EISSN: None     Source Type: Journal    
DOI: 10.1093/oxfordjournals.pcp.a029233     Document Type: Article

References (48)

1. Banjoko, A. and Trelease, R.N. (1995) Development and application of an in vivo plant peroxisome import system. Plant Physiol. 107: 1201-1208.
2. Beeching, J.R. and Northcote, D.H. (1987) Nucleic acid (cDNA) and amino acid sequences of isocitrate lyase from castor bean. Plant. Mol. Biol. 8: 471-475.
3. Beevers, H. (1979) Microbodies in higher plants. Annu. Rev. Plant Physiol. 30: 159-193.
4. Comai, L., Baden, C.S. and Harada, J.J. (1989) Deduced sequence of a malate synthase polypeptide encoded by a subclass of the gene family. J. BM. Chem. 264: 2778-2782.
5. De Bellis, L., Tsugeki, R. and Nishimura, M. (1991) Glyoxylate cycle enzymes in peroxisomes isolated from petals of pumpkin (Cucurbita sp.) during senescence. Plant Cell Physiol. 32: 1227-1235.
6. Fransen, M., Brees, C., Baumgart, E., Vanhooren, J.C.T., Baes, M., Mannaerts, G.P. and Vanveldhoven, P.P. (1995) Identification and characterization of the putative human peroxisomal C-terminal targeting signal import receptor. J. Biol. Chem. 270: 7731-7736.
7. Gietl, C. (1990) Glyoxysomal malate dehydrogenase from watermelon is synthesized with an amino-terminal transit peptide. Proc. Natl. Acad. Sci. USA 87: 5773-5777.
8. Gould, S.J., Keller, G.A., Hosken, N., Wilkinson, J. and Subramani, S. (1989) A conserved tripeptide sorts proteins to peroxisomes. J. Cell. Biol. 108: 1657-1664.
9. Could, S. J., Keller, G.A. and Subramani, S. (1988) Identification of peroxisomal targeting signals located at the carboxy terminus of four peroxisomal proteins. J. Cell. Biol. 107: 897-905.
10. Gould, S.J., Keller, G.-A.A. and Subramani, S. (1987) Identification of a peroxisomal targeting signal at the carboxy terminus of firefly luciferase. J. Cell. Biol. 105:2923-2931.
11. Graham, I.A., Smith, L.M., Brown, J.W., Leaver, C.J. and Smith, S.M. (1989) The malate synthase gene of cucumber. Plant Mol. Biol. 13: 673-684.
12. Hayashi, M., Aoki, M., Kato, A., Kondo, M. and Nishimura, M. (1996a) Transport of chimeric proteins that contain a carboxy-terminal targeting signal into plant microbodies. Plant J. 10: 225-234.
13. Hayashi, M., De Bellis, L., Alpi, A. and Nishimura, M. (1995) Cytosolic aconitase participates in the glyoxylate cycle in etiolated pumpkin cotyledons. Plant Cell Physiol. 36: 669-680.
14. Hayashi, M., Tsugeki, R., Kondo, M., Mori, H. and Nishimura, M. (1996b) Pumpkin hydroxypyruvate reductases with and without a putative C-terminal signal for targeting to microbodies may be produced by alternative splicing. Plant Mol. Biol. 30: 183-189.
15. Huang, A.H.C., Trelease, R.N. and Moore, T.S. (1983) Plant Peroxisomes. New York: NY: Academic Press.
16. Kato, A., Hayashi, M., Kondo, M. and Nishimura, M. (1996a) Targeting and processing of a chimeric protein with the amino-terminal presequence of the precursor to glyoxysomal citrate synthase. Plant Cell 8: 1601-1611.
17. Kato, A., Hayashi, M., Mori, H. and Nishimura, M. (1995) Molecular characterization of a glyoxysomal citrate synthase that is synthesized as a precursor of higher molecular mass in pumpkin. Plant Mol. Biol. 27: 377-390.
18. Kato, A., Hayashi, M., Takeuchi, Y. and Nishimura, M. (1996b) cDNA cloning and expression of a gene for 3-ketoacyl-CoA thiolase in pumpkin cotyledons. Plant Mol. Biol. 31: 843-852.
19. Mano, S., Hayashi, M., Kondo, M. and Nishimura, M. (1996) cDNA cloning and expression of the isocitrate lyase gene in pumpkin cotyledons. Plant Cell Physiol. 37: 941-948.
20. Marchuk, D., Drumm, M., Saulino, A. and Collins, F.S. (1990) Construction of T-vectors, a rapid and general system for direct cloning of unmodified PCR products. Nucl. Acids Res. 19: 1154.
21. Matsuoka, K. and Nakamura, K. (1991) Propeptide of a precursor to a plant vacuolar protein required for vacuolar targeting. Proc. Natl. Acad. Sci. USA 88: 834-838.
22. Mori, H. and Nishimura, M. (1989) Glyoxysomal malate synthase is specifically degraded in microbodies during greening of pumpkin cotyledons. FEBS Lett. 244: 163-166.
23. Mori, H., Takeda, Y.Y., Hara-Nishimura, I. and Nishimura, M. (1991) Pumpkin malate synthase: cloning and sequencing of the cDNA and Northern blot analysis. Eur. J. Biochem. 197: 331-336.
24. Nagel, A., Elliot, A., Masel, A., Birch, R.G. and Manners, J.M. (1990) Electroporation of binary Ti plasmid vector into Agrobacterium tumefaciens and Agrobacterium rhizogenes. FEMS Microbiol. Lett. 67: 325-328.
25. Nguyen, T., Zelechowska, M., Foster, V., Bergmann, H. and Verma, D. (1985) Primary structure of the soybean nodulin-35 gene encoding uricase II localized in the peroxisomes of uninfected cell of nodules. Proc. Natl. Acad. Sci. USA 82: 5040-5044.
26. Nishimura, M., Takeuchi, Y., De Bellis, L. and Hara-Nishimura, I. (1993) Leaf peroxisomes are directly transformed to glyoxysomes during senescence of pumpkin cotyledons. Protoplasma 175: 131-137.
27. Nishimura, M., Yamaguchi, J., Mori, H., Akazawa, T. and Yokota, S. (1986) Immunocytochemical analysis shows that glyoxysomes are directly transformed to leaf peroxisomes during greening of pumpkin cotyledons. Plant Physiol. 80: 313-316.
28. Olsen, L.J., Ettinger, W.F., Damsz, B., Matsudaira, K., Webb, M.A. and Harada, J.J. (1993) Targeting of glyoxysomal proteins to peroxisomes in leaves and roots of a higher plant. Plant Cell 5: 941-952.
29. Olsen, L.J. and Harada, J.I. (1995) Peroxisomes and their assembly in higher plants. Anna. Rev. Plant Physiol. Plant MoI. Biol. 46: 123-146.
30. Onyeocha, I., Behari, R., Hill, D. and Baker, A. (1993) Targeting of castor bean glyoxysomal isocitrate lyase to tobacco leaf peroxisomes. Plant Mol. Biol. 22: 385-396.
31. Preisig-Muller, R., Guhnemann-Schafer, K. and Kindl, H. (1994) Domains of the tetrafunctional protein acting in glyoxysomal fatty acid beta-oxidation. Demonstration of epimerase and isomerase activities on a peptide lacking hydratase activity. J. Biol. Chem. 269: 20475-20481.
32. Preisig-Muller, R. and Kindl, H. (1993) Thiolase mRNA translated in vitro yields a peptide with a putative N-terminal presequence. Plant Mol. Biol. 22: 59-66.
33. Purdue, P.E. and Lazarow, P.B. (1994) Peroxisomal biogenesis: multiple pathways of protein import. J. Biol. Chem. 269: 30065-30068.
34. Rodriguez, D., Ginger, R.S., Baker, A. and Northcote, D.H. (1990) Nucleotide sequence analysis of a cDNA clone encoding malate synthase of castor bean (Ricinus communis) reveals homology to DAL7, a gene involved in allantoin degradation in Saccharomyces cerevisiae. Plant Mol. Biol. 15: 501-504.
35. Sambrook, J., Fritsch, E.F. and Maniatis, T. (1989) Molecular Cloning: a Laboratory Manual, 2nd ed. Cold Spring Harbor, NY: Cold Spring Harbor Laboratory.
36. Swinkels, B.W., Gould, S.J. and Subramani, S. (1992) Targeting efficiencies of various permutations of the consensus C-terminal tripeptide peroxisomal targeting signal. FEBS Lett. 305: 133-136.
37. Terlecky, S.R., Nuttley, W.M., McCollum, D., Sock, E. and Subramani, S. (1995) The Pichia pastoris peroxisomal protein PASSp is the receptor for the C-terminal tripeptide peroxisomal targeting signal. EMBO J. 14: 3627-3634.
38. Titus, D.E. and Becker, W.M. (1985) Investigation of the glyoxysome-peroxisome transition in germinating cucumber cotyledons using double-label immunoelectron microscopy. J. Cell. Biol. 101: 1288-1299.
39. Trelease, R.N., Choe, S.M. and Jacobs, B.L. (1994) Conservative amino acid substitutions of the C-terminal tripeptide (Ala-Arg-Met) on cotton-seed isocitrate lyase preserve import in vivo into mammalian cell peroxisomes. Eur. J. Cell Biol. 65: 269-279.
40. Tsugeki, R., Hara-Nishimura, I., Mori, H. and Nishimura, M. (1993) Cloning and sequencing of cDNA for glycolate oxidase from pumpkin cotyledons and Northern blot analysis. Plant Cell Physiol. 34: 51-57.
41. Turley, R.B., Choe, S.M., Ni, W. and Trelease, R.N. (1990a) Nucleotide sequence of cottonseed malate synthase. Nucl. Acids Res. 18: 3643.
42. Turley, R.B., Choe, S.M. and Trelease, R.N. (1990b) Characterization of a cDNA clone encoding the complete amino acid sequence of cotton isocitrate lyase. Biochim. Biophys. Acta 1049: 223-226.
43. Valvekens, K., Montagu, M.V. and Lijsebettens, M.V. (1988) Agrobacterium tumefaciens-mediated transformation of Arabidopsis thaliana root expiants by using kanamycin selection. Proc. Natl. Acad. Sci. USA 85: 5536-5540.
44. Vanderleij, I., Franse, M.M., Elgersma, Y., Distel, B. and Tabak, H.F. (1993) PAS10 is a Tetratricopeptide-Repeat Protein That is Essential for the Import of Most Matrix Proteins into Peroxisomes of Saccharomyces cerevisiae. Proc. Natl. Acad. Sci. USA 90: 11782-11786.
45. Volokita, M. (1991) The carboxy-terminal end of glycolate oxidase directs a foreign protein into tobacco leaf peroxisomes. Plant J. 1: 361-366.
46. Volokita, M. and Somerville, C.R. (1987) The primary structure of spinach glycolate oxidase deduced from the DNA sequence of a cDNA clone. J. Biol. Chem. 262: 15825-15828.
47. Yamaguchi, J. and Nishimura, M. (1984) Purification of glyoxysomal catalase and immunochemical comparison of glyoxysomal and leaf peroxisomal catalase in germinating pumpkin cotyledons. Plant Physiol. 74: 261-267.
48. Zhang, J.Z., Gomezpedrozo, M., Baden, C.S. and Harada, JJ. (1993) 2 Classes of isocitrate lyase genes are expressed during late embryogeny and postgermination in Brassica napus L. Mol. Gen. Genet. 238: 177-184.