Isolation and characterisation of a cDNA encoding a novel cytosolic ascorbate peroxidase from potato plants [Solanum tuberosum L.]

• Autorzy: Soares da Costa D , Pereira C.S. , Teixeira J. , Pereira S.
• Języki publikacji: EN

Abstrakty

EN

Ascorbate peroxidase (APX) is one of the key enzymes of the plant antioxidant system playing, along with catalase, a central role in hydrogen per oxidescavenging. An approach to further in crease the knowledge about cytosolic APX gene organization can be achieved by isolating and characterisating new cDNAs, thus providing new in sights about the physiological roles and regula tion of these enzymes. A partial cDNA clone (corresponding to the 3’ untranslated region), cytosolic ascorbate peroxidase-re lated, was isolated from potato sprouts by RT-PCR. Data base analysis re trieved several expressed sequence tags (ESTs) coding potato cytosolic ascorbate peroxidase, that were used to infer the complete cDNA sequence. The deduced amino acid sequence revealed high homologies with other plant cytosolic ascorbate peroxidases, con firming the reliability of the vir tual cDNA. Northern blot analysis revealed the existence of a single band related to the isolated cDNA and the southern blotting results al lowed the elaboration of a possible gene organization.

Słowa kluczowe

EN

Solanum tuberosum; cDNA encoding; northern blotting; southern blotting; potato plant; cDNA isolation; ascorbate peroxidase

• Wydawca: -
• Czasopismo: Acta Physiologiae Plantarum
• Rocznik: 2006
• Tom: 28
• Numer: 1
• Opis fizyczny: p.41-47,fig.,ref.

Twórcy

autor

Soares da Costa D

• University of Porto, Rua do Campo Alegre, 823, 4150-180 - Porto, Portugal

autor

Pereira C.S.

autor

Teixeira J.

autor

Pereira S.

Bibliografia

• Çelic A., Cullis P., Sutcliffe M., Sangar R. and Raven E. 2001. Engineering the active site of ascorbate peroxidase. Eur. J. Biochem. 268: 78-85.
• Corpas F., Bunkelmann J. and Trelease R. 1994. Identification and immunochemical characterisation of a family of peroxisome membrane proteins (PMPs) in oil seed glyoxisomes. Eur. J. Cell Biol. 65: 280-290.
• De Leonardis S., Dipierro N. and Dipierro S. 2000. Purification and characterization of an ascorbate peroxidase from potato tuber mitochondria. Plant Physiol. Biochem., 38: 773-779.
• Del Rio L., Corpas F., Sandalio L., Palma J., Gómez M. and Barroso J. 2002. Reactive oxygen species, antioxidant systems and nitric oxide in peroxisomes. Journal of Exp. Botany, 53: 372: 1255-1272.
• Doyle J. J., Doyle J. L. 1990. Isolation of plant DNA from fresh tissue. Focus 12: 13–15.
• Gadea J., Conejero V., Vera P. 1999. Developmental regulation of a cytosolic ascorbate peroxidase gene from tomato plants. Mol. Gen. Genet.; 262: 212-219.
• Ishikawa T., Sakai K., Takeda T. and Shigeoka S. 1995. Clon ing and exoression of cDNA en cod ing a new type of ascorbate peroxidase from spinach. FEBS Letters 367: 28-32.
• Ishikawa T., Sakai K., Yoshimura K., Takeda T., Shigeoka S. 1996. cDNAs encoding spinach stromal and thylakoid-bound ascorbate peroxidase, differing in the presence or absence of their 3’-coding regions. FEBS Let ters 384: 289-293.
• Ishikawa T., Yoshimura K., Sakai K., Tamoi M., Takeda T. and Shigeoka S. 1998. Molecular characterization and physiological role of a glyoxisome-bound ascorbate peroxidase from spinach. Plant Cell Physiol., 30: 23-34.
• Jespersen H., Kjaersgard I., Ostergaard L. and Welinder K. 1997. From sequence analysis of three novel ascorbate peroxidases from Arabidopsis thaliana to structure, function and evolution of seven types of ascorbate peroxidase. Biochem. Journal, 326: 305-310.
• Kawakami S., Matsumoto Y., Matsunaga A., Mayama S. and Mizuno M. 2002. Molecular cloning of ascorbate peroxidase in potato tubers and its response during storage at low temperature. Plant Science, 163: 829-836.
• Lad L., Mewies M., Basran J., Scrutton N. and Raven E. 2002. Role of histidine 42 in ascorbate peroxidase - Kinetic analysis of the H42A and H42E variants. Eur. J. Biochem. 269: 3182–3192.
• Lisenbee C., Heinze M. and Trelease R. 2003. Peroxisomal ascorbate peroxidase re sides within a subdomain of rough endoplasmic reticulum in wild-type Arabidopsis cells. Plant Physiol., 132: 870-882.
• Mittler R. and Zilinskas B. 1992. Molecular cloning and characterization of a gene encoding pea cytosolic ascorbate peroxidase. The Journal of Biological Chemistry, 267, 30: 21802-21807.
• Mittler R. e Zilinskas B.A. 1991. Molecular cloning and nucleotide sequence analysis of cDNA en coding pea cytosolic ascorbate peroxidase. FEBS letters-289: 257-259.
• Morita S., Kaminaka H., Yokoi H., Masumura T. and Tanaka K. 1997. Cloning and characterization of cytosolic ascorbate peroxidase cDNA from rice. Plant Physiol., 113: 306.
• Orvar B. and Ellis B. 1995. Isolation of a cDNA encoding cytosolic ascorbate peroxidase in To bacco. Plant Physiol., 108: 839-840.
• Patterson W. and Poulos T. 1994. Characterization and Crystallization of Recombinant Pea Cytosolic Ascorbate Peroxidase. J. Biol. Chem. 269: 17020-17024.
• Shigeoka S., Ishikawa T., Tamoi M., Miyagawa Y., Takeda T., Yabuta Y. and Yoshimura K. 2002. Regula tion and function of ascorbate peroxidase isoenzymes. Journal of Exp. Botany, 53, 372, 1305-1319.
• Webb R. and Allen R. 1995. Isolation and characterization of a cDNA for spinach cytosolic ascorbate peroxidase. Plant Physiol., 108: 1325.
• Zhang H., Wang J., Nicke U., Allen R and Good man H. 1997. Cloning and expression of an Arabidopsis gene encoding a putative peroxisomal ascorbate peroxidase. Plant Molecular Biology 34: 967–971.