Chaperone activity of ERD10 and ERD14, two disordered stress-related plant proteins

Plant Physiology

Volumn 147, Issue 1, 2008, Pages 381-390

  Kovacs, Denes ^a   Kalmar, Eva ^b   Torok, Zsolt ^c   Tompa, Peter ^a  

^a INSTITUTE OF EXPERIMENTAL MEDICINE   (Hungary)

^b SEMMELWEIS UNIVERSITY   (Hungary)

^c INSTITUTE OF BIOCHEMISTRY   (Hungary)

Author keywords

[No Author keywords available]

Indexed keywords

ARABIDOPSIS; ARABIDOPSIS THALIANA;

ALCOHOL DEHYDROGENASE; ARABIDOPSIS PROTEIN; CHAPERONE; CITRATE SYNTHASE; ERD10 PROTEIN, ARABIDOPSIS; ERD14 PROTEIN, ARABIDOPSIS; FIREFLY LUCIFERASE; LATE EMBRYOGENESIS ABUNDANT PROTEIN, PLANT; LYSOZYME; VEGETABLE PROTEIN; WATER;

ARABIDOPSIS; ARTICLE; ENZYME SPECIFICITY; HEAT; INTRACELLULAR MEMBRANE; METABOLISM; PHYSIOLOGY;

ALCOHOL DEHYDROGENASE; ARABIDOPSIS; ARABIDOPSIS PROTEINS; CITRATE (SI)-SYNTHASE; HEAT; INTRACELLULAR MEMBRANES; LUCIFERASES, FIREFLY; MOLECULAR CHAPERONES; MURAMIDASE; PLANT PROTEINS; SUBSTRATE SPECIFICITY; WATER;

EID: 50649098927     PISSN: 00320889     EISSN: 15322548     Source Type: Journal    
DOI: 10.1104/pp.108.118208     Document Type: Article

References (62)

1. Ahn M, Kim S, Kang M, Ryu Y, Kim TD (2006) Chaperone-like activities of alpha-synuclein: Alpha-synuclein assists enzyme activities of esterases. Biochem Biophys Res Commun 346: 1142-1149
2. Alsheikh MK, Heyen BJ, Randall SK (2003) Ion binding properties of the dehydrin ERD14 are dependent upon phosphorylation. J Biol Chem 278: 40882-40889
3. Alsheikh MK, Svensson JT, Randall SK (2005) Phosphorylation regulated ion-binding is a property shared by the acidic subclass dehydrins. Plant Cell Environ 28: 1114-1122
4. Arnold K, Hoekstra D, Ohki S (1992) Association of lysozyme to phospholipid surfaces and vesicle fusion. Biochim Biophys Acta 1124: 88-94
5. Asghar R, Fenton R, DeMason D, Close T (1994) Nuclear and cytoplasmic localization of maize embryo and aleurone dehydrin. Protoplasma 177: 87-94
6. Bokor M, Csizmok V, Kovacs D, Banki P, Friedrich P, Tompa P, Tompa K (2005) NMR relaxation studies on the hydrate layer of intrinsically unstructured proteins. Biophys J 88: 2030-2037
7. Chakrabortee S, Boschetti C, Walton LJ, Sarkar S, Rubinsztein DC, Tunnacliffe A (2007) Hydrophilic protein associated with desiccation tolerance exhibits broad protein stabilization function. Proc Natl Acad Sci USA 104: 18073-18078
8. Chen J, Song JL, Zhang S, Wang Y, Cui DF, Wang CC (1999) Chaperone activity of DsbC. J Biol Chem 274: 19601-19605
9. Close TJ (1996) Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97: 795-803
10. Danyluk J, Perron A, Houde M, Limin A, Fowler B, Benhamou N, Sarhan F (1998) Accumulation of an acidic dehydrin in the vicinity of the plasma membrane during cold acclimation of wheat. Plant Cell 10: 623-638
11. Dosztanyi Z, Csizmok V, Tompa P, Simon I (2005) IUPred: web server for the prediction of intrinsically unstructured regions of proteins based on estimated energy content. Bioinformatics 21: 3433-3434
12. Dyson HJ, Wright PE (2004) Unfolded proteins and protein folding studied by NMR. Chem Rev 104: 3607-3622
13. Dyson HJ, Wright PE (2005) Intrinsically unstructured proteins and their functions. Nat RevMol Cell Biol 6: 197-208
14. Egerton-Warburton L, Balsamo R, Close T (1997) Temporal accumulation and ultrastructural localization of dehydrins in Zea mays L. Physiol Plant 101: 545-555
15. Goyal K, Tisi L, Basran A, Browne J, Burnell A, Zurdo J, Tunnacliffe A (2003) Transition from natively unfolded to folded state induced by desiccation in an anhydrobiotic nematode protein. J Biol Chem 278: 12977-12984
16. Goyal K, Walton LJ, Tunnacliffe A (2005) LEA proteins prevent protein aggregation due to water stress. Biochem J 388: 151-157
17. Guha S, Manna TK, Das KP, Bhattacharyya B (1998) Chaperone-like activity of tubulin. J Biol Chem 273: 30077-30080
18. Hara M, Terashima S, Kuboi T (2001) Characterization and cryoprotective activity of cold-responsive dehydrin from Citrus unshiu. J Plant Physiol 158: 1333-1339
19. Heyen BJ, Alsheikh MK, Smith EA, Torvik CF, Seals DF, Randall SK (2002) The calcium-binding activity of a vacuole-associated, dehydrinlike protein is regulated by phosphorylation. Plant Physiol 130: 675-687
20. HoudeM, Danyluk J, Laliberte JF, Rassart E, Dhindsa RS, Sarhan F (1992) Cloning, characterization, and expression of a cDNA encoding a 50-kilodalton protein specifically induced by cold acclimation in wheat. Plant Physiol 99: 1381-1387
21. Ismail AM, Hall AE, Close TJ (1999a) Allelic variation of a dehydrin gene cosegregates with chilling tolerance during seedling emergence. Proc Natl Acad Sci USA 96: 13566-13570
22. Ismail AM, Hall AE, Close TJ (1999b) Purification and partial characterization of a dehydrin involved in chilling tolerance during seedling emergence of cowpea. Plant Physiol 120: 237-244
23. Johansson K, Bourhis JM, Campanacci V, Cambillau C, Canard B, Longhi S (2003) Crystal structure of the measles virus phosphoprotein domain responsible for the induced folding of the C-terminal domain of the nucleoprotein. J Biol Chem 278: 44567-44573
24. Kim TD, Paik SR, Yang CH, Kim J (2000) Structural changes in alpha-synuclein affect its chaperone-like activity in vitro. Protein Sci 9: 2489-2496
25. Kimura M, Yamamoto YY, Seki M, Sakurai T, Sato M, Abe T, Yoshida S, Manabe K, Shinozaki K, Matsui M (2003) Identification of Arabidopsis genes regulated by high light-stress using cDNA microarray. Photochem Photobiol 77: 226-233
26. Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K (1994a) Characterization of two cDNAs (ERD10 and ERD14) corresponding to genes that respond rapidly to dehydration stress in Arabidopsis thaliana. Plant Cell Physiol 35: 225-231
27. Kiyosue T, Yamaguchi-Shinozaki K, Shinozaki K (1994b) Cloning of cDNAs for genes that are early-responsive to dehydration stress (ERDs) in Arabidopsis thaliana L.: identification of three ERDs as HSP cognate genes. Plant Mol Biol 25: 791-798
28. Koag MC, Fenton RD, Wilkens S, Close TJ (2003) The binding of maize DHN1 to lipid vesicles: gain of structure and lipid specificity. Plant Physiol 131: 309-316
29. Leung J, Giraudat J (1998) Abscisic acid signal transduction. Annu Rev Plant Physiol Plant Mol Biol 49: 199-222
30. Li R, Brawley SH, Close TJ (1998) Proteins immunologically related to dehydrins in fucoid algae. J Phycol 34: 642-650
31. Mayer LD, Hope MJ, Cullis PR (1986) Vesicles of variable sizes produced by a rapid extrusion procedure. Biochim Biophys Acta 858: 161-168
32. McCubbin WD, Kay CM, Lane BG (1985) Hydrodynamic and optical properties of the wheat germ Em protein. Can J Biochem Cell Biol 63: 803-811
33. Meszaros B, Tompa P, Simon I, Dosztanyi Z (2007) Molecular principles of the interactions of disordered proteins. J Mol Biol 372: 549-561
34. Minami M, Nakamura M, Emori Y, Minami Y (2001) Both the N- and C-terminal chaperone sites of Hsp90 participate in protein refolding. Eur J Biochem 268: 2520-2524
35. Momma M, Kaneko S, Haraguchi K, Matsukura U (2003) Peptide mapping and assessment of cryoprotective activity of 26/27-kDa dehydrin from soybean seeds. Biosci Biotechnol Biochem 67: 1832-1835
36. Mouillon JM, Gustafsson P, Harryson P (2006) Structural investigation of disordered stress proteins: comparison of full-length dehydrins with isolated peptides of their conserved segments. Plant Physiol 141: 638-650
37. Nylander M, Svensson J, Palva ET, Welin BV (2001) Stress-induced accumulation and tissue-specific localization of dehydrins in Arabidopsis thaliana. Plant Mol Biol 45: 263-279
38. Ohki S, Marcus E, Sukumaran DK, Arnold K (1994) Interaction of melittin with lipid membranes. Biochim Biophys Acta 1194: 223-232
39. Oldfield CJ, Cheng Y, Cortese MS, Brown CJ, Uversky VN, Dunker AK (2005) Comparing and combining predictors of mostly disordered proteins. Biochemistry 44: 1989-2000
40. Receveur-Brechot V, Bourhis JM, Uversky VN, Canard B, Longhi S (2005) Assessing protein disorder and induced folding. Proteins 62: 24-45
41. Richard S, Morency MJ, Drevet C, Jouanin L, Seguin A (2000) Isolation and characterization of a dehydrin gene from white spruce induced upon wounding, drought and cold stresses. Plant Mol Biol 43: 1-10
42. Romero P, Obradovic Z, Dunker AK (2004) Natively disordered proteins: functions and predictions. Appl Bioinformatics 3: 105-113
43. Rorat T (2006) Plant dehydrins: tissue location, structure and function. Cell Mol Biol Lett 11: 536-556
44. Saavedra L, Svensson J, Carballo V, Izmendi D, Welin B, Vidal S (2006) A dehydrin gene in Physcomitrella patens is required for salt and osmotic stress tolerance. Plant J 45: 237-249
45. Sambrook J, Fritsch EF, Maniatis T (1989) Isolation of DNA from mammalian cells. In N Ford, C Nolan, and M Ferguson, eds, Molecular Cloning: A Laboratory Manual, Ed 2, Vol 2. Cold Spring Harbor Laboratory Press, Woodbury, NY, p 9.16
46. Schlame M, Horvath I, Torok Z, Horvath LI, Vigh L (1990) Intramembraneous hydrogenation of mitochondrial lipids reduces the substrate availability, but not the enzyme activity of endogenous phospholipase A. The role of polyunsaturated phospholipid species. Biochim Biophys Acta 1045: 1-8
47. Shinozaki K, Yamaguchi-Shinozaki K (1996) Molecular responses to drought and cold stress. Curr Opin Biotechnol 7: 161-167
48. Soulages JL, Kim K, Arrese EL, Walters C, Cushman JC (2003) Conformation of a group 2 late embryogenesis abundant protein from soybean: evidence of poly (L-proline)-type II structure. Plant Physiol 131: 963-975
49. Souza JM, Giasson BI, Lee VM, Ischiropoulos H (2000) Chaperone-like activity of synucleins. FEBS Lett 474: 116-119
50. Svensson J, Palva ET, Welin B (2000) Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expr Purif 20: 169-178
51. Tamminen I, Makela P, Heino P, Palva ET (2001) Ectopic expression of ABI3 gene enhances freezing tolerance in response to abscisic acid and low temperature in Arabidopsis thaliana. Plant J 25: 1-8
52. Tompa P (2002) Intrinsically unstructured proteins. Trends Biochem Sci 27: 527-533
53. Tompa P, Banki P, Bokor M, Kamasa P, Kovacs D, Lasanda G, Tompa K (2006) Protein-water and protein-buffer interactions in the aqueous solution of an intrinsically unstructured plant dehydrin: NMR intensity and DSC aspects. Biophys J 91: 2243-2249
54. Tompa P, Csermely P (2004) The role of structural disorder in the function of RNA and protein chaperones. FASEB J 18: 1169-1175
55. Tompa P, Dosztanyi Z, Simon I (2006) Prevalent structural disorder in E. coli and S. cerevisiae proteomes. J Proteome Res 5: 1996-2000
56. Tompa P, Emori Y, Sorimachi H, Suzuki K, Friedrich P (2001) Domain III of calpain is a Ca2+-regulated phospholipid-binding domain. Biochem Biophys Res Commun 280: 1333-1339
57. Tompa P, Szasz C, Buday L (2005) Structural disorder throws new light on moonlighting. Trends Biochem Sci 30: 484-489
58. Torok Z, Horvath I, Goloubinoff P, Kovacs E, Glatz A, Balogh G, Vigh L (1997) Evidence for a lipochaperonin: association of active protein-folding GroESL oligomers with lipids can stabilize membranes under heat shock conditions. Proc Natl Acad Sci USA 94: 2192-2197
59. Tunnacliffe A, Wise MJ (2007) The continuing conundrum of the LEA proteins. Naturwissenschaften 94: 791-812
60. Welin BV, Olson A, Nylander M, Palva ET (1994) Characterization and differential expression of dhn/lea/rab-like genes during cold acclimation and drought stress in Arabidopsis thaliana. Plant Mol Biol 26: 131-144
61. Wise MJ, Tunnacliffe A (2004) POPP the question: What do LEA proteins do? Trends Plant Sci 9: 13-17
62. Wisniewskia M, Webba R, Balsamob R, Closec T, Yud X, Griffiths M (1999) Purification, immunolocalization, cryoprotective, and antifreeze activity of PCA60: a dehydrin from peach (Prunus persica). Physiol Plant 105: 600-608