Proteomics of extreme freezing tolerance in Siberian spruce (Picea obovata)

Journal of Proteomics

Volumn 73, Issue 5, 2010, Pages 965-975

  Kjellsen, Trygve D ^a   Shiryaeva, Liudmila ^b   Schröder, Wolfgang P ^b   Strimbeck, G Richard ^a  

^a NORWEGIAN UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Norway)

^b UMEÅ UNIVERSITY   (Sweden)

Author keywords

Dehydrins; DIGE; Freezing tolerance; MALDI TOF TOF; OPLS DA; Picea obovata

Indexed keywords

ADENOSINE TRIPHOSPHATASE; ALTEPLASE; CYCLOPHILIN; DEHYDRIN; GLUTAMATE AMMONIA LIGASE; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; HEAT SHOCK PROTEIN 70; LIPOCALIN; MALATE DEHYDROGENASE; METHIONINE SULFOXIDE REDUCTASE; NUCLEOSIDE DIPHOSPHATE SUGAR; PROTEOME; REACTIVE OXYGEN METABOLITE; RIBULOSEBISPHOSPHATE CARBOXYLASE; UNCLASSIFIED DRUG;

ABIOTIC STRESS; ACCLIMATIZATION; ARTICLE; BIOACCUMULATION; BIOTIC STRESS; FREEZING TOLERANCE; LOW TEMPERATURE; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; NONHUMAN; PHOTOSYSTEM II; PICEA OBOVATA; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN EXPRESSION; PROTEOMICS; SPRUCE; TIME OF FLIGHT MASS SPECTROMETRY; TWO DIMENSIONAL GEL ELECTROPHORESIS;

ACCLIMATIZATION; CLUSTER ANALYSIS; FREEZING; GENE EXPRESSION PROFILING; GENE EXPRESSION REGULATION, PLANT; PICEA; PLANT PROTEINS; PROTEOMICS; SEASONS;

CONIFEROPHYTA; PICEA; PICEA OBOVATA;

EID: 77249098683     PISSN: 18743919     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jprot.2009.12.010     Document Type: Article

References (57)

1. Renaut J., Hausman J.F., Bassett C., Artlip T., Cauchie H.M., Witters E., et al. Quantitative proteomic analysis of short photoperiod and low-temperature responses in bark tissues of peach (Prunus persica L. Batsch). Tree Genet Genomes 4 (2008) 589-600
2. Amme S., Matros A., Schlesier B., and Mock H.P. Proteome analysis of cold stress response in Arabidopsis thaliana using DIGE-technology. J Exp Bot 57 (2006) 1537-1546
3. Strimbeck G.R., Kjellsen T.D., Schaberg P.G., and Murakami P.F. Dynamics of low-temperature acclimation in temperate and boreal conifer foliage in a mild winter climate. Tree Physiol 28 (2008) 1365-1374
4. Welling A., Rinne P., Vihera-Aarnio A., Kontunen-Soppela S., Heino P., and Palva E.T. Photoperiod and temperature differentially regulate the expression of two dehydrin genes during overwintering of birch (Betula pubescens Ehrh.). J Exp Bot 55 (2004) 507-516
5. Öquist G. Seasonally induced changes in acyl lipids and fatty acids of chloroplast thylakoids of pinus silvestris: a correletion between the level of unsaturation of monogalactosyldiglyceride and the rate of electron transport. Plant Physiol 69 (1982) 869-875
6. Quinn P.J. A lipid-phase separation model of low-temperature damage to biological-membranes. Cryobiology 22 (1985) 128-146
7. Steponkus P.L., Lynch D.V., and Uemura M. The influence of cold-acclimation on the lipid-composition and cryobehavior of the plasma-membrane of isolated rye protoplasts. Philos Trans R Soc Lond Ser B-Biol Sci 326 (1990) 571-583
8. Close T.J. Dehydrins: a commonality in the response of plants to dehydration and low temperature. Physiol Plant 100 (1997) 291-296
9. Shinozaki K., and Yamaguchi-Shinozaki K. Molecular responses to dehydration and low temperature: differences and cross-talk between two stress signaling pathways. Curr Opin Plant Biol 3 (2000) 217-223
10. Bigras F.J., and Colombo S.J. Conifer cold hardiness (2001), Kluwer Academic Publishers, Dordrecht
11. Hansen J., and Beck E. Seasonal-changes in the utilization and turnover of assimilation products in 8-year-old scots pine (Pinus-sylvestris L) trees. Trees-Struct Funct 8 (1994) 172-182
12. Frankow-Lindberg B.E. Adaptation to winter stress in nine white clover populations: changes in non-structural carbohydrates during exposure to simulated winter conditions and 'spring' regrowth potential. Ann Bot 88 (2001) 745-751
13. Tao D.L., Oquist G., and Wingsle G. Active oxygen scavengers during cold acclimation of Scots pine seedlings in relation to freezing tolerance. Cryobiology 37 (1998) 38-45
14. Rappsilber J., and Mann M. What does it mean to identify a protein in proteomics?. Trends Biochem Sci 27 (2002) 74-78
15. Selles-Marchart S., Luque I., Casado-Vela J., Martinez-Esteso M.J., and Bru-Martinez R. Proteomics of multigenic families from species underrepresented in databases: the case of loquat (Eriobotrya japonica Lindl.) polyphenol oxidases. J Proteome Res 7 (2008) 4095-4106
16. Gottlieb D.M., Schultz J., Bruun S.W., Jacobsen S., and Sondergaard I. Multivariate approaches in plant science. Phytochemistry 65 (2004) 1531-1548
17. Strimbeck G.R., Kjellsen T.D., Schaberg P.G., and Murakami P.F. Cold in the common garden: comparative low-temperature tolerance of boreal and temperate conifer foliage. Trees-Struct Funct 21 (2007) 557-567
18. Moen A. National Atlas of Norway:vegetation (1999), Norwegian Mapping Authority, Hønefoss
19. Wang W., Vignani R., Scali M., and Cresti M. A universal and rapid protocol for protein extraction from recalcitrant plant tissues for proteomic analysis. Electrophoresis 27 (2006) 2782-2786
20. Bradford M.M. Rapid and sensitive method for quantitation of microgram quantities of protein utilizing principle of protein-dye binding. Anal Biochem 72 (1976) 248-254
21. Kravchenko A.N., Larionova A.Y., and Milyutin L.I. Genetic polymorphism of siberian spruce (Picea obovata ledeb.) in middle Siberia. Russ J Genet 44 (2008) 35-43
22. Close T.J. Dehydrins: emergence of a biochemical role of a family of plant dehydration proteins. Physiol Plant 97 (1996) 795-803
23. Svensson J., Palva E.T., and Welin B. Purification of recombinant Arabidopsis thaliana dehydrins by metal ion affinity chromatography. Protein Expr Purif 20 (2000) 169-178
24. Rinne P.L., Kaikuranta P.L., van der Plas L.H., and van der Schoot C. Dehydrins in cold-acclimated apices of birch (Betula pubescens ehrh.): production, localization and potential role in rescuing enzyme function during dehydration. Planta 209 (1999) 377-388
25. Soulages J.L., Kim K., Arrese E.L., Walters C., and Cushman J.C. Conformation of a group 2 late embryogenesis abundant protein from soybean. Evidence of poly (L-proline)-type II structure. Plant Physiol 131 (2003) 963-975
26. Rorat T. Plant dehydrins-tissue location, structure and function. Cell Mol Biol Lett 11 (2006) 536-556
27. Buitink J., and Leprince O. Glass formation in plant anhydrobiotes: survival in the dry state. Cryobiology 48 (2004) 215-228
28. Burke M.J. In: Leopold A.C. (Ed). The glassy state and survival of anhydrous biological systems. Membranes metabolism and dry organisms (1986), Cornell University Press, Ithaca, NY 358-364
29. Marian C.O., Krebs S.L., and Arora R. Dehydrin variability among rhododendron species: a 25-kDa dehydrin is conserved and associated with cold acclimation across diverse species. New Phytol 161 (2004) 773-780
30. Renaut J., Hoffmann L., and Hausman J.F. Biochemical and physiological mechanisms related to cold acclimation and enhanced freezing tolerance in poplar plantlets. Physiol Plant 125 (2005) 82-94
31. Arora R., and Wisniewski M.E. Cold-acclimation in genetically related (sibling) deciduous and evergreen peach (Prunus-persica [L] Batsch) .2. A 60-kilodalton bark protein in cold-acclimated tissues of peach is heat-stable and related to the dehydrin family of proteins. Plant Physiol 105 (1994) 95-101
32. Rinne P., Welling A., and Kaikuranta P. Onset of freezing tolerance in birch (Betula pubescens Ehrh.) involves LEA proteins and osmoregulation and is impaired in an ABA-deficient genotype. Plant Cell Environ 21 (1998) 601-611
33. Kontunen-Soppela S., and Laine K. Seasonal fluctuation of dehydrins is related to osmotic status in Scots pine needles. Trees-Struct Funct 15 (2001) 425-430
34. Hartl F.U. Molecular chaperones in cellular protein folding. Nature 381 (1996) 571-580
35. Frydman J. Folding of newly translated proteins in vivo: the role of molecular chaperones. Annu Rev Biochem 70 (2001) 603-647
36. Wisniewski M., Close T.J., Artlip T., and Arora R. Seasonal patterns of dehydrins and 70-kDa heat-shock proteins in bark tissues of eight species of woody plants. Physiol Plant 96 (1996) 496-505
37. Anderson J.V., Li Q.B., Haskell D.W., and Guy C.L. Structural organization of the spinach endoplasmic reticulum-luminal 70-kilodalton heat-shock cognate gene and expression of 70-kilodalton heat-shock genes during cold-acclimation. Plant Physiol 104 (1994) 1359-1370
38. Neuwald A.F., Aravind L., Spouge J.L., and Koonin E.V. AAA(+): a class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes. Genome Res. 9 (1999) 27-43
39. Ito K., and Akiyama Y. Cellular functions, mechanism of action, and regulation of FtsH protease. Annu. Rev. Microbiol. 59 (2005) 211-231
40. Martz F., Sutinen M.L., Kivineemi S., and Palta J.P. Changes in freezing tolerance, plasma membrane H+-ATPase activity and fatty acid composition in Pinus resinosa needles during cold acclimation and de-acclimation. Tree Physiol 26 (2006) 783-790
41. Arora R., and Palta J.P. A loss in the plasma-membrane atpase activity and its recovery coincides with incipient freeze-thaw injury and postthaw recovery in onion bulb scale tissue. Plant Physiol. 95 (1991) 846-852
42. Charron J.B.F., Ouellet F., Pelletier M., Danyluk J., Chauve C., and Sarhan F. Identification, expression, and evolutionary analyses of plant lipocalins. Plant Physiol 139 (2005) 2017-2028
43. Charron J.B.F., Ouellet F., Houde M., and Sarhan F. The plant apolipoprotein D ortholog protects Arabidopsis against oxidative stress. BMC Plant Biol 8 (2008)
44. Galat A. Variations of sequences and amino acid compositions of proteins that sustain their biological functions: an analysis of the cyclophilin family of proteins. Arch Biochem Biophys 371 (1999) 149-162
45. Bozhko M., Riegel R., Schubert R., and Muller-Starck G. A cyclophilin gene marker confirming geographical differentiation of Norway spruce populations and indicating viability response on excess soil-born salinity. Mol Ecol 12 (2003) 3147-3155
46. Romano P., Gray J., Horton P., and Luan S. Plant immunophilins: functional versatility beyond protein maturation. New Phytol 166 (2005) 753-769
47. Brandts J.F., Halvorson H.R., and Brennan M. Consideration of possibility that slow step in protein denaturation reactions is due to cis-trans isomerism of proline residues. Biochemistry 14 (1975) 4953-4963
48. Gopalan G., He Z., Balmer Y., Romano P., Gupta R., Héroux A., et al. Structural analysis uncovers a role for redox in regulating FKBP13, an immunophilin of the chloroplast thylakoid lumen. Proc Natl Acad Sci U S A 101 (2004) 13945-13950
49. Romano P.G.N., Horton P., and Gray J.E. The Arabidopsis cyclophilin gene family. Plant Physiol 134 (2004) 1268-1282
50. Kieselbach T., and Schroder W.P. The proteome of the chloroplast lumen of higher plants. Photosynth Res 78 (2003) 249-264
51. Kenan D.J., Query C.C., and Keene J.D. Rna recognition-towards identifying determinants of specificity. Trends Biochem Sci 16 (1991) 214-220
52. Richard S., Drevet C., Jouanin L., and Seguin A. Isolation and characterization of a cDNA clone encoding a putative white spruce glycine-rich RNA binding protein. Gene 240 (1999) 379-388
53. Mittler R. Oxidative stress, antioxidants and stress tolerance. Trends Plant Sci 7 (2002) 405-410
54. Yan J.Q., Wang J., and Zhang H. An ankyrin repeat-containing protein plays a role in both disease resistance and antioxidation metabolism. Plant J 29 (2002) 193-202
55. Plucken H., Muller B., Grohmann D., Westhoff P., and Eichacker L.A. The HCF136 protein is essential for assembly of the photosystem II reaction center in Arabidopsis thaliana. FEBS Lett 532 (2002) 85-90
56. Ottander C., Campbell D., and Oquist G. Seasonal-changes in photosystem-II organization and pigment composition in Pinus-sylvestris. Planta 197 (1995) 176-183
57. Aro E.M., Virgin I., and Andersson B. Photoinhibition of photosystem-2-inactivation, protein damage and turnover. Biochim Biophys Acta 1143 (1993) 113-134