Expansin

Expansin refers to a family of closely related nonenzymatic proteins found in the plant cell wall, with important roles in plant cell growth, fruit softening, abscission, emergence of root hairs, pollen tube invasion of the stigma and style, meristem function, and other developmental processes where cell wall loosening occurs.[1] Expansins were originally discovered as mediators of acid growth, which refers to the widespread characteristic of growing plant cell walls to expand faster at low (acidic) pH than at neutral pH.[2] Expansins are thus linked to auxin action. They are also linked to cell enlargement and cell wall changes induced by other plant hormones such as gibberellin,[3] cytokinin,[4] ethylene[5] and brassinosteroids.[6]

A subset of the β-expansins are also the major group-1 allergens of grass pollens.[7]

Families

So far, two large families of expansin genes have been discovered in plants, named alpha-expansins (given the gene symbol EXPA) and beta-expansins (EXPB). Both families of expansins have been identified in a wide range of land plants, from angiosperms and gymnosperms to ferns and mosses. The model plant Arabidopsis thaliana contains around 26 different α-expansin genes and 6 β-expansin genes. A subset of β-expansins has evolved a special role in grass pollen, where they are known as group 1 grass pollen allergens.[7] Plants also have a small set of expansin-like genes (named EXLA and EXLB) whose function has not been established.[8] Some proteins in bacteria and fungi are known to have distant sequence similarity to plant expansins.[9][10][11] Strong evidence that at least some of these sequences are indeed expansins came in 2008[12] when the crystal structure of the YOAJ protein from a bacterium (Bacillus subtilis) was shown to be very similar to the structure of plant expansins, despite the low sequence similarity. This study also noted that proteins related to YOAJ were found in diverse species of plant pathogenic bacteria, but not in related bacteria that did not attack or colonize plants, thus suggesting that these bacterial expansins have a role in plant-microbe interactions. Some animals can too produce a functional expansin, such as Globodera rostochiensis, a plant-parasitic nematode, which uses it to loosen cell walls when invading its host plant.[13]

To be designated as expansin or expansin-like, genes and their protein products must contain both domain I (N-terminal, catalytic, GH45-like - GH meaning glycoside-hydrolase) and domain II (C-terminal, distantly related to group-2 grass pollen allergens).[8][14] Non-plant expansins can be designated with the symbol EXLX (expansin-like X), but they do not constitute to a monophyletic group;[8] distantly similar to plant expansins,[9] they could have diverged prior to the origin of land plants, or else could have been acquired by horizontal transfer.

Nomenclature of genes and proteins of expansins and expansin-like: e.g., Arabidopsis thaliana EXPANSIN A1 is named "AtEXPA1" as for the gene, and "AtEXPA1" as for the protein; one adds "-1" for mutant allele 1.

Actions

Expansins characteristically cause wall stress relaxation and irreversible wall extension (wall creep).[15] This process is essential for cell enlargement. Expansins are also expressed in ripening fruit where they function in fruit softening,[16] and in grass pollen,[7] where they loosen stigmatic cell walls and aid pollen tube penetration of the stigmain germinating seeds for cell wall disassembly,[17] in floral organs for their patterning, in developing nitrogen-fixing nodules in legumes, in abscissing leaves, in parasitic plants, and in ‘resurrection’ plants during their rehydration. No enzymatic activity has been found for expansin and in particular, no glucanase activity: they don't hydrolyze the matrix polysaccharides;[15] the only definitive assay for expansin activity is thus to measure wall stress relaxation or wall extension.

Structure and regulation

Expansins are proteins; the two expansins initially uncovered had molecular weights of 29 kDa (kiloDalton) and 30 kDa,[2] which would correspond to around 270 amino acids on average. Generally speaking, α- and β-expansins and expansin-like are composed of approximately 300 amino acids,[9] with a MW of ~25–28 kDa for the mature protein. The peptidic sequence of an expansin consists, in particular, of: a signal peptide of around 20–30 amino acids at the N-terminal end, the putative catalytic domain, a His-Phe-Asp (HFD) motif in central region (except EXL), and the C-terminal putative cellulose-binding domain with conserved Trp (tryptophan) residues. Sequence analysis of expansin genes shows seven introns named A, B, C, D, E, F, and G; sequences from different expansin genes show good correspondence, the exon/intron organization being conserved among α- and β-expansins, and expansin-like genes,[18] although the number of introns and the length of each intron differ among genes. In the N-terminal signal sequences of α-expansin genes, the general absence of endoplasmic reticulum retention signal (KDEL or HDEL) confirms that the proteins are targeted to the cell wall. A promoter analysis of expansin genes indicates that expression of these genes may be regulated by auxin, gibberellin, cytokinin or ethylene, this being more frequent in α-expansins than in β-expansins; semi-aquatic plants such as Rumex palustris, which are induced to grow rapidly by submergence, show a transcription induction by submergence, the same as in rice where hypoxia and submergence increase α-expansin mRNA levels.[18]

Mechanism

The plant cell wall has high tensile strength and must be loosened to enable the cell to grow (enlarge irreversibly).[19] Within the cell wall, this expansion of surface area involves slippage or movement of cellulose microfibrils, which normally is coupled to simultaneous uptake of water. In physical terms, this mode of wall expansion requires cell turgor pressure to stretch the cell wall and put the network of interlinked cellulose microfibrils under tension. By loosening the linkages between cellulose microfibrils, expansins allow the wall to yield to the tensile stresses created in the wall through turgor pressure. The molecular mechanism by which expansin loosens the cellulosic network within the cell wall is not yet established in detail. However, expansin is hypothesized to disrupt the non-covalent adhesion or entrapment of hemicellulose on the surface of cellulose microfibrils. Hemicelluloses can tether cellulose microfibrils together, forming a strong load-bearing network. Expansin is thought to disrupt the cellulose-hemicellulose association transiently, allowing slippage or movement of cell wall polymers before the association reforms and the integrity of the cell wall network is reestablished.[20]

Turning to the function of bacterial expansins, the bacterial protein named YOAJ or BsEXLX1 binds to plant and bacterial cell walls and has weak but significant expansin activity,[12] that is, it induces plant cell wall extension in vitro. Moreover, B. subtilis mutants lacking BsEXLX1 were defective in colonizing plant roots, suggesting that this protein facilitates plant-bacterium interactions.

Allergenicity

In grass pollens, the major allergens (group-1 allergens, main causative agents of hay fever and of seasonal asthma) are structurally linked to a sub-group of the β-expansins.[7] These expansins appear specialized in pollination, likely in loosening the cell walls of the maternal tissues during penetration of the pollen tube into the stigma and style, as is suggested by their potent rheological effect on grass style and stigma walls, where they are abundantly released by the pollen. Expansin-like proteins are implicated in group-2 and -3 grass allergenes, less important than those of group-1. These three allergens groups share a carbohydrate-binding module (CBM), which could be responsible for the binding to the IgE antibody.[21] The expansin domain II, causative of the allergenic effects, could be related to the competition between pollens for access to ovules.[22]

See also

References

  1. Cosgrove DJ (September 2000). "Loosening of plant cell walls by expansins" (PDF). Nature. 407 (6802): 321–6. doi:10.1038/35030000. PMID 11014181.
  2. 1 2 McQueen-Mason S, Durachko DM, Cosgrove DJ (November 1992). "Two endogenous proteins that induce cell wall extension in plants". Plant Cell. 4: 1425–33. doi:10.2307/3869513. PMC 160229Freely accessible. PMID 11538167.
  3. Cho HT, Kende H (September 1997). "Expression of expansin genes is correlated with growth in deepwater rice". Plant Cell. 9 (9): 1661–71. doi:10.1105/tpc.9.9.1661. PMC 157041Freely accessible. PMID 9338967.
  4. Downes BP, Crowell DN (June 1998). "Cytokinin regulates the expression of a soybean β-expansin gene by a post-transcriptional mechanism" (PDF). Plant Mol. Biol. 37 (3): 437–44. doi:10.1023/A:1005920732211. PMID 9617811.
  5. Cho HT, Cosgrove DJ (December 2002). "Regulation of root hair initiation and expansin gene expression in Arabidopsis". Plant Cell. 14 (12): 3237–53. doi:10.1105/tpc.006437. PMC 151215Freely accessible. PMID 12468740.
  6. Sun Y, Veerabomma S, Abdel-Mageed HA, et al. (August 2005). "Brassinosteroid regulates fiber development on cultured cotton ovules". Plant Cell Physiol. 46 (8): 1384–91. doi:10.1093/pcp/pci150. PMID 15958497.
  7. 1 2 3 4 Cosgrove DJ, Bedinger P, Durachko DM (June 1997). "Group I allergens of grass pollen as cell wall-loosening agents". Proc. Natl. Acad. Sci. U.S.A. 94 (12): 6559–64. doi:10.1073/pnas.94.12.6559. PMC 21089Freely accessible. PMID 9177257.
  8. 1 2 3 Sampedro, J.; Cosgrove, D.J. (2005). "The expansin superfamily". Genome Biol. 6 (12): 242. doi:10.1186/gb-2005-6-12-242. PMC 1414085Freely accessible. PMID 16356276.
  9. 1 2 3 Li Y, Darley CP, Ongaro V, et al. (March 2002). "Plant expansins are a complex multigene family with an ancient evolutionary origin". Plant Physiol. 128 (3): 854–64. doi:10.1104/pp.010658. PMC 152199Freely accessible. PMID 11891242.
  10. Saloheimo M, Paloheimo M, Hakola S, et al. (September 2002). "Swollenin, a Trichoderma reesei protein with sequence similarity to the plant expansins, exhibits disruption activity on cellulosic materials". Eur. J. Biochem. 269 (17): 4202–11. doi:10.1046/j.1432-1033.2002.03095.x. PMID 12199698.
  11. Laine MJ, Haapalainen M, Wahlroos T, Kankare K, Nissinen R, Kassuwi S, Metzler MC (November 2000). "The cellulase encoded by the native plasmid of Clavibacter michiganensis ssp. sepedonicus plays a role in virulence and contains an expansin-like domain". Physiol Mol Plant Pathol. 57 (5): 221–233. doi:10.1006/pmpp.2000.0301.
  12. 1 2 Kerff F, Amoroso A, Herman R, et al. (November 2008). "Crystal structure and activity of Bacillus subtilis YoaJ (EXLX1), a bacterial expansin that promotes root colonization". Proc. Natl. Acad. Sci. U.S.A. 105 (44): 16876–81. doi:10.1073/pnas.0809382105. PMC 2579346Freely accessible. PMID 18971341.
  13. Qin L, Kudla U, Roze EH, et al. (January 2004). "Plant degradation: a nematode expansin acting on plants". Nature. 427 (6969): 30. doi:10.1038/427030a. PMID 14702076.
  14. Kende H, Bradford K, Brummell D (May 2004). "Nomenclature for members of the expansin superfamily of genes and proteins". Plant Mol. Biol. 55 (3): 311–4. doi:10.1007/s11103-004-0158-6. PMID 15604683.
  15. 1 2 McQueen-Mason SJ, Cosgrove DJ (January 1995). "Expansin mode of action on cell walls. Analysis of wall hydrolysis, stress relaxation, and binding". Plant Physiol. 107 (1): 87–100. doi:10.1104/pp.107.1.87. PMC 161171Freely accessible. PMID 11536663.
  16. Rose JK, Lee HH, Bennett AB (May 1997). "Expression of a divergent expansin gene is fruit-specific and ripening-regulated". Proc. Natl. Acad. Sci. U.S.A. 94 (11): 5955–60. doi:10.1073/pnas.94.11.5955. PMC 20888Freely accessible. PMID 9159182.
  17. Chen F, Bradford KJ (November 2000). "Expression of an expansin is associated with endosperm weakening during tomato seed germination". Plant Physiol. 124 (3): 1265–74. doi:10.1104/pp.124.3.1265. PMC 59224Freely accessible. PMID 11080302.
  18. 1 2 Lee Y, Choi D, Kende H (December 2001). "Expansins: ever-expanding numbers and functions". Curr. Opin. Plant Biol. 4 (6): 527–32. doi:10.1016/S1369-5266(00)00211-9. PMID 11641069.
  19. Cosgrove, D.J. (November 2005). "Growth of the plant cell wall" (PDF). Nat. Rev. Mol. Cell Biol. 6 (11): 850–61. doi:10.1038/nrm1746. PMID 16261190.
  20. Yennawar NH, Li LC, Dudzinski DM, Tabuchi A, Cosgrove DJ (October 2006). "Crystal structure and activities of EXPB1 (Zea m 1), a β-expansin and group-1 pollen allergen from maize". Proc. Natl. Acad. Sci. U.S.A. 103 (40): 14664–71. doi:10.1073/pnas.0605979103. PMC 1595409Freely accessible. PMID 16984999.
  21. Shani N, Shani Z, Shoseyov O, Mruwat R, Shoseyov D (January 2011). "Oxidized cellulose binding to allergens with a carbohydrate-binding module attenuates allergic reactions". J. Immunol. 186 (2): 1240–7. doi:10.4049/jimmunol.1000640. PMID 21169552.
  22. Valdivia ER, Wu Y, Li LC, Cosgrove DJ, Stephenson AG (2007). "A group-1 grass pollen allergen influences the outcome of pollen competition in maize". PLoS ONE. 2 (1): e154. doi:10.1371/journal.pone.0000154. PMC 1764715Freely accessible. PMID 17225858.
This article is issued from Wikipedia - version of the 5/24/2016. The text is available under the Creative Commons Attribution/Share Alike but additional terms may apply for the media files.