Expression of Pisum sativum SAD polypeptides in production hosts and in planta: Tetrameric organization of the protein

Protein Expression and Purification

Volumn 63, Issue 1, 2009, Pages 18-25

  Scherbak, Nikolai ^a   Brosché, Mikael ^b   Ala Häivälä, Anneli ^a   Strid, Hilja ^a   Öhrfelt, Annika ^b,c   Nilsson, Fredrik ^c   Strid, Åke ^a  

^a ÖREBRO UNIVERSITY   (Sweden)

^b UNIVERSITY OF GOTHENBURG   (Sweden)

^c ASTRAZENECA R AND D   (Sweden)

Author keywords

Environmental stress; Short chain alcohol dehydrogenase; Short chain dehydrogenase reductase; Tetramer; Ultraviolet B radiation

Indexed keywords

ALCOHOL DEHYDROGENASE; MESSENGER RNA; RECOMBINANT PROTEIN; SADA PROTEIN, PISUM SATIVUM; SADB PROTEIN, PISUM SATIVUM; SADC PROTEIN, PISUM SATIVUM; VEGETABLE PROTEIN;

ARTICLE; CHEMISTRY; ELECTROSPRAY MASS SPECTROMETRY; GENE EXPRESSION; GENETICS; ISOLATION AND PURIFICATION; LIQUID CHROMATOGRAPHY; MASS SPECTROMETRY; METABOLISM; MOLECULAR CLONING; NORTHERN BLOTTING; PEA; PLANT GENE; PROTEIN QUATERNARY STRUCTURE; ULTRAVIOLET RADIATION; WESTERN BLOTTING;

ALCOHOL DEHYDROGENASE; BLOTTING, NORTHERN; BLOTTING, WESTERN; CHROMATOGRAPHY, LIQUID; CLONING, MOLECULAR; GENE EXPRESSION; GENES, PLANT; PEAS; PLANT PROTEINS; PROTEIN STRUCTURE, QUATERNARY; RECOMBINANT PROTEINS; RNA, MESSENGER; SPECTROMETRY, MASS, ELECTROSPRAY IONIZATION; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; ULTRAVIOLET RAYS;

ESCHERICHIA COLI; ORYCTOLAGUS CUNICULUS; PICHIA PASTORIS; PISUM SATIVUM;

EID: 54849413351     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.09.004     Document Type: Article

References (37)

1. Brosché M., and Strid A. Cloning, expression, and molecular characterization of a small pea gene family regulated by low levels of ultraviolet B radiation and other stresses. Plant Physiol. 121 (1999) 479-487
2. Kalbin G., Hidema J., Brosché M., Kumagai T., Bornman J.F., and Strid A. UV-B-induced DNA damage and expression of defence genes under UV-B stress: tissue-specific molecular marker analysis in leaves. Plant Cell Environ. 24 (2001) 983-990
3. Gittins J.R., Schuler M.A., and Strid A. Identification of a novel nuclear factor-binding site in the Pisum sativum sad gene promoters. Biochim. Biophys. Acta 1574 (2002) 231-244
4. Finsterbusch A., Lindemann P., Grimm R., Eckerskorn C., and Luckner M. Δ(5)-3β-Hydroxysteroid dehydrogenase from Digitalis lanata Ehrh. - a multifunctional enzyme in steroid metabolism?. Planta 209 (1999) 478-486
5. Xia Z., Costa M.A., Pélissier H.C., Davin L.B., and Lewis N.G. Secoisolariciresinol dehydrogenase purification, cloning and functional expression. J. Biol. Chem. 276 (2001) 12614-12623
6. Jacobsen S.E., and Olszewski N.E. Gibberellins regulate the abundance of RNAs with sequence similarity to proteinase inhibitors, dioxygenases and dehydrogenases. Planta 198 (1996) 78-86
7. DeLong A., Calderon-Urrea A., and Dellaporta S.L. Sex determination gene TASSELSEED2 of maize encodes a short-chain alcohol dehydrogenase required for stage-specific floral organ abortion. Cell 74 (1993) 757-768
8. Jörnvall H., Persson B., and Jeffery J. Alcohol and polyol dehydrogenases are both divided into two protein types, and structural properties cross-relate the different enzyme activities within each type. Proc. Natl. Acad. Sci. USA 78 (1981) 4226-4230
9. Kallberg Y., Oppermann U., Jörnvall H., and Persson B. Short-chain dehydrogenases/reductases (SDRs). Coenzyme-based functional assignments in completed genomes. Eur. J. Biochem. 269 (2002) 4409-4417
10. Rosati F., Giovanna D., Guarna A., Cini N., Rachi M.L., and Serio M. New evidence of similarity between human and plant steroid metabolism: 5α-reductase activity in Solanum malacoxylon. Endocrinology 144 (2003) 220-229
11. Bachem C.W.B., Horvath B., Trindade L., Claassens M., Davelaar E., Jordi W., and Visser R.G.F. A potato tuber-expressed mRNA with homology to steroid dehydrogenases affects gibberrellin levels and plant development. Plant J. 25 (2001) 595-604
12. Bollenbach T.J., and Stern D.B. Secondary structures common to chloroplast mRNA 3' UTRs direct cleavage by CSP41, an endoribonuclease belonging to the short chain dehydrogenase/reductase superfamily. J. Biol. Chem. 278 (2003) 25832-25838
13. Ringer K.L., Davis E.M., and Croteau R. Monoterpene metabolism. Cloning, expression, and characterization of (-)-isopiperitenol/(-)-carveol dehydrogenase of peppermint and spearmint. Plant Physiol. 137 (2005) 863-872
14. Youn B., Moinuddin S.G., Davin L.B., Lewis N.G., and Kang C. Crystal structures of apo-form and binary/ternary complexes of Podophyllum secoisolariciresinol dehydrogenase, an enzyme involved in formation of health-protecting and plant defense lignans. J. Biol. Chem. 280 (2005) 12917-12926
15. Persson B., Kallberg Y., Oppermann U., and Jörnvall H. Coenzyme-based functional assignments of short-chain dehydrogenases/reductases (SDRs). Chem. Biol. Interact. 143-144 (2003) 271-278
16. Studier F.W., Rosenberg A.H., Dunn J.J., and Dubendorff J.W. Use of T7 RNA polymerase to direct expression of cloned genes. Methods Enzymol. 185 (1989) 60-89
17. D.R. Hoagland, D.I. Arnon, The water-culture method for growing plants without soil, in: California Agricultural Experiment Station Circular 347. The College of Agriculture, University of California, Berkeley, CA, 1950.
18. Caldwell M.M. (1971)Solar UV irradiation and the growth and development of higher plants in photobiology. In: Giese A.C. (Ed). Currents Topics in Photobiology and Photochemistry vol. 6 (1971), Academic Press, New York 131-177
19. Green A.E.S., Sawada T., and Shettle E.P. The middle ultraviolet reaching the ground. Photochem. Photobiol. Sci. 19 (1974) 251-259
20. Strid A., Chow W.S., and Anderson J.M. Changes in the relaxation of electrochromic shifts of photosynthetic pigments and in the levels of mRNA transcripts in leaves of Pisum sativum as a result of mRNA exposure to supplementary UV-B radiation. The dependency on the intensity of the photosynthetically active radiation. Plant Cell Physiol. 37 (1996) 61-67
21. Sävenstrand H., Brosché M., Ängehagen M., and Strid A. Molecular markers for ozone stress isolated by suppression subtractive hybridization: specificity of gene expression and identification of a novel stress-regulated gene. Plant Cell Environ. 23 (2000) 689-700
22. Kalbin G., Ohlsson A.B., Berglund T., Rydström J., and Strid A. Ultraviolet-B-radiation-induced changes in nicotinamide and glutathi, one metabolism and gene expression in plants. Eur. J. Biochem. 249 (1997) 465-472
23. Jörnvall H., Persson B., Krook M., Atrian S., Gonzales-Duarte R., Jeffrey J., and Ghosh D. Short-chain dehydrogenases/reductases (SDR). Biochemistry 34 (1995) 6003-6013
24. Oppermann U., Filling C., Hult M., Shafqat N., Wu X., Lindh M., Shafqat J., Nordling E., Kallberg Y., Persson B., and Jörnvall H. Short-chain dehydrogenases/reductases (SDR): the 2002 update. Chem. Biol. Interact. 143-144 (2003) 247-253
25. Ghosh D., Pletnev V.Z., Zhu D.-W., Wawrzak Z., Duax W.L., Pangborn W., Labrie F., and Lin S.-X. Structure of human estrogenic 17β-hydroxysteroid dehydrogenase at 2.20 Å resolution. Structure 3 (1995) 503-513
26. Ghosh D., Wawrzak Z., Weeks C.M., Duax W.L., and Erman M. The refined three-dimensional structure of 3α,20β-hydroxysteroid dehydrogenase and possible roles of the residues conserved in short-chain dehydrogenases. Structure 2 (1994) 629-640
27. Ghosh D., Sawicki M., Pletnev V., Erman M., Ohno S., Nakajin S., and Duax W. Porcine carbonyl reductase. Structural basis for a functional monomer in short chain dehydrogenases/reductases. J. Biol. Chem. 276 (2001) 18457-18463
28. Brosché M., and Strid A. Molecular events following perception of ultraviolet-B radiation by plants. Physiol. Plant. 117 (2003) 1-10
29. Li J., Ou-Lee T.M., Raba R., Amundson R.G., and Last R.L. Arabidopsis flavonoid mutants are hypersensitive to UV-B irradiation. Plant Cell 5 (1993) 171-179
30. Chow W.S., Strid A., and Anderson J.M. Short-term treatment of pea plants with supplementary ultraviolet-B radiation: recovery time-courses of some photosynthetic functions and components. In: Murata N. (Ed). Research in Photosynthesis vol. IV (1992), Kluwer Academic Publishers, Dordrecht, The Netherlands 361-364
31. Mackerness S.A.-H., John C.F., Jordan B.R., and Thomas B. Early signalling components in ultraviolet-B responses: distinct roles for different reactive oxygen species and nitric oxide. FEBS Lett. 489 (2001) 237-242
32. Mackerness S.A.-H. Plant responses to ultraviolet-B (UV-B: 280-320 nm) stress: what are the key regulators?. Plant Growth Regul. 37 (2000) 27-39
33. Sävenstrand H., Brosché M., and Strid A. Ultraviolet-B signalling: arabidopsis brassinosteroid mutants are defective in UV-B regulated defence gene expression. Plant Physiol. Biochem. 42 (2004) 687-694
34. De Jong R.M., Tiesinga J.J.W., Roseboom H.J., Kalk K.H., Tang L., Janssen D.B., and Dijkstra B.W. Structure and mechanism of bacterial haloalcohol dehalogenase: a new variation of the short-chain dehydrogenase/reductase fold without an NAD(P)H binding site. EMBO J. 22 (2003) 4933-4944
35. Stammers D.K., Ren J., Leslie K., Nichols C.E., Lamb H.K., Cocklin S., Dodds A., and Hawkins A.R. The structure of the negative transcriptional regulator MnrA reveals a structural superfamily which includes the short-chain dehydrogenase/reductase. EMBO J. 20 (2001) 6619-6626
36. Baker M.E., Yan L., and Pear M.R. Three-dimensional model of human TIP30, a cofactor for HIV-1 Tat-activated transcription and CC3, a protein associated with metastasis suppression. Cell. Mol. Life Sci. 57 (2000) 851-858
37. El Omari K., Bird L.E., Nichols C.E., Ren J., and Stammers D.K. Crystal structure of CC3 (TIP30). Implications for its role as a tumor suppressor. J. Biol. Chem. 280 (2005) 18229-18236