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Plant peptide hormone

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Peptide signaling plays a significant role in various aspects of plant growth and development and specific receptors for various peptides have been identified as being membrane-localized receptor kinases, the largest family of receptor-like molecules in plants. Signaling peptides include members of the following protein families.

  • Systemin — is a small polypeptide functioning as a long-distance signal to activate chemical defenses against herbivores. It was the first plant hormone proven to be a peptide. Systemin induces the production of protein defense compound called protease inhibitors. Systemin was first identified in tomato leaves. It was found to be an 18-amino acid peptide processed from the C-terminus of a 200-amino acid precursor, which is called prosystemin.[1]
  • CLV3/ESR-related ('CLE') peptide family — CLV3 encodes a small secreted peptide that functions as a short range ligand to the membrane-bound CLV1 receptor like kinase that together with CLV2 (a receptor-like protein) function to maintain stem cell homeostasis in Arabidopsis shoot apical meristems. Although the maize embryo-surrounding region protein (ESR).[2] and CLV3 are very different, they are both members of the CLE peptide family given that they share a short conserved 14-amino acid sequence at the carboxy terminal region.[3] To date, more than 150 CLE signaling peptides are identified.[4][5] This proteolytically processed bioactive region is important for both promoting and inhibiting cellular differentiation in both apical and cambial meristems.[6]
  • ENOD40 — is an early nodulin gene, hence ENOD, that putatively encodes two small peptides, one of 12 and the other of 18 amino acid residues. Controversy exists on whether the mRNA or peptides themselves are responsible for bioactivity.[7][8][9][10] Both peptides have been shown "in vivo" to bind to the 93 kDa subunit of sucrose synthase, an essential component in sucrose metabolism.[8] Sucrose degradation is a key step in nitrogen fixation, and is a pre-requisite for normal nodule development.[11]
  • Phytosulfokine (PSK) — was first identified as a "conditioning factor" in asparagus and carrot cell cultures.[12][13] The bioactive five amino acid peptide (PSK) is proteolytically processed from an ~80 amino acid precursor secreted peptide.[14] PSK has been demonstrated to promote cellular proliferation and transdifferentiation. It has been demonstrated that PSK binds to a membrane bound LRR receptor like kinase (PSKR).[15]
  • POLARIS (PLS) — The PLS peptide has a predicted length of 36 amino acids however possesses no secretion signal, suggesting that it functions within the cytoplasm. The PLS peptide itself has not yet been biochemically isolated, however loss-of-function mutants are hypersensitive to cytokinin with reduced responsiveness to auxin. Developmentally it is involved in vascularization, longitudinal cell expansion and increased radial expansion.[16]
  • Rapid Alkalinization Factor (RALF) — is 49 amino acid peptide that was identified whilst purifying systemin from tobacco leaves, it causes rapid medium alkanalization and does not activate defence responses like systemin.[17] Tomato RALF precursor cDNA encodes a 115 amino acid polypeptide containing an amino-terminal signal sequence with the bioactive RALF peptide encoded at the carboxy terminus. It is not known how mature RALF peptide is produced from its precursor, but a dibasic amino acid motif (typical of recognition sites of processing enzymes in yeast and animals) is located two residues upstream from the amino terminus of mature RALF. RALF has been identified to bind to potential membrane bound receptors complex containing proteins 25 kDa and 120 kDa in size.[18]
  • SCR/SP11 — are small polymorphic peptides produced by the tapetal cells of anthers and is involved in self-incompatibility of Brassica species.[19][20][21] This secreted polypeptide is between 78 and 80 amino acid residues in length. Unlike other peptide hormones, no further post-translational processing occurs, except for the removal of the N-terminal signal peptide. SCR/SP11 like other small peptide hormones binds to a membrane bound LRR receptor like kinase (SRK).[22][23]
  • ROTUNDIFOLIA4/DEVIL1 (ROT4/DVL1) — The ROT4 and DVL1 are peptides of 53 and 51 amino acids respectively, which have a high degree of sequence homology. They are two members of 23 member peptide family. ROT4 and DVL1 are involved in regulating polar cell proliferation on the longitudinal axis of organs.[24][25]
  • Inflorescence deficient in abscission (IDA) — a family of secreted peptides identified to be involved in petal abscission. The peptides are 77 amino acids in length and possess an amino-terminal secretions signal. Like the CLE peptide family these proteins have a conserved carboxy-terminal domain that is bordered by potentially cleavable basic residues. These proteins are secreted from cells in the floral abscission zone.[26] Studies suggest that the HAESA membrane-associated LRR-RLK is likely to be this peptide's receptor as it too is expressed in the zone of floral organ abscission.[27]

See also

References

  1. ^ McGurl B, Pearce G, Orozco-Cardenas M, Ryan CA (March 1992). "Structure, expression, and antisense inhibition of the systemin precursor gene". Science. 255 (5051): 1570–3. doi:10.1126/science.1549783. PMID 1549783.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  2. ^ Opsahl-Ferstad HG, Le Deunff E, Dumas C, Rogowsky PM (July 1997). "ZmEsr, a novel endosperm-specific gene expressed in a restricted region around the maize embryo". Plant J. 12 (1): 235–46. doi:10.1046/j.1365-313x.1997.12010235.x. PMID 9263463.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  3. ^ Sharma VK, Ramirez J, Fletcher JC (February 2003). "The Arabidopsis CLV3-like (CLE) genes are expressed in diverse tissues and encode secreted proteins" (PDF). Plant Mol. Biol. 51 (3): 415–25. doi:10.1023/A:1022038932376. PMID 12602871.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  4. ^ Cock JM, McCormick S (July 2001). "A large family of genes that share homology with CLAVATA3". Plant Physiol. 126 (3): 939–42. doi:10.1104/pp.126.3.939. PMC 1540125. PMID 11457943.
  5. ^ Oelkers K, Goffard N, Weiller GF, Gresshoff PM, Mathesius U, Frickey T (2008). "Bioinformatic analysis of the CLE signaling peptide family". BMC Plant Biol. 8: 1. doi:10.1186/1471-2229-8-1. PMC 2254619. PMID 18171480.{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
  6. ^ Whitford R, Fernandez A, De Groodt R, Ortega E, Hilson P (November 2008). "Plant CLE peptides from two distinct functional classes synergistically induce division of vascular cells". Proc. Natl. Acad. Sci. U.S.A. 105 (47): 18625–30. doi:10.1073/pnas.0809395105. PMC 2587568. PMID 19011104.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  7. ^ Campalans A, Kondorosi A, Crespi M (April 2004). "Enod40, a short open reading frame-containing mRNA, induces cytoplasmic localization of a nuclear RNA binding protein in Medicago truncatula". Plant Cell. 16 (4): 1047–59. doi:10.1105/tpc.019406. PMC 412876. PMID 15037734.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  8. ^ a b Röhrig H, John M, Schmidt J (December 2004). "Modification of soybean sucrose synthase by S-thiolation with ENOD40 peptide A". Biochem. Biophys. Res. Commun. 325 (3): 864–70. doi:10.1016/j.bbrc.2004.10.100. PMID 15541370.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  9. ^ Rohrig H, Schmidt J, Miklashevichs E, Schell J, John M (February 2002). "Soybean ENOD40 encodes two peptides that bind to sucrose synthase". Proc. Natl. Acad. Sci. U.S.A. 99 (4): 1915–20. doi:10.1073/pnas.022664799. PMC 122294. PMID 11842184.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  10. ^ Guzzo F, Portaluppi P, Grisi R, et al. (February 2005). "Reduction of cell size induced by enod40 in Arabidopsis thaliana". J. Exp. Bot. 56 (412): 507–13. doi:10.1093/jxb/eri028. PMID 15557291.
  11. ^ Gordon AJ, Minchin FR, James CL, Komina O (July 1999). "Sucrose synthase in legume nodules is essential for nitrogen fixation". Plant Physiol. 120 (3): 867–78. doi:10.1104/pp.120.3.867. PMC 59326. PMID 10398723.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  12. ^ Bellincampi D, Morpurgo G (1987). "Conditioning factor affecting growth in plant cells in culture". Plant Sci. 51: 83–91. doi:10.1016/0168-9452(87)90223-8.
  13. ^ Birnberg PR, Somers DA, Brenner ML (1988). "Characterization of conditioning factors that increase colony formation from black Mexican sweet corn protoplasts". J. Plant Physiol. 132: 316–21. doi:10.1016/s0176-1617(88)80113-5.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  14. ^ Yang H, Matsubayashi Y, Nakamura K, Sakagami Y (November 1999). "Oryza sativa PSK gene encodes a precursor of phytosulfokine-alpha, a sulfated peptide growth factor found in plants". Proc. Natl. Acad. Sci. U.S.A. 96 (23): 13560–5. doi:10.1073/pnas.96.23.13560. PMC 23987. PMID 10557360.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  15. ^ Matsubayashi Y, Sakagami Y (May 2000). "120- and 160-kDa receptors for endogenous mitogenic peptide, phytosulfokine-alpha, in rice plasma membranes". J. Biol. Chem. 275 (20): 15520–5. doi:10.1074/jbc.275.20.15520. PMID 10809784.{{cite journal}}: CS1 maint: unflagged free DOI (link)
  16. ^ Topping JF, Lindsey K (October 1997). "Promoter trap markers differentiate structural and positional components of polar development in Arabidopsis". Plant Cell. 9 (10): 1713–25. doi:10.1105/tpc.9.10.1713. PMC 157016. PMID 9368412.
  17. ^ Pearce G, Moura DS, Stratmann J, Ryan CA (October 2001). "RALF, a 5-kDa ubiquitous polypeptide in plants, arrests root growth and development". Proc. Natl. Acad. Sci. U.S.A. 98 (22): 12843–7. doi:10.1073/pnas.201416998. PMC 60141. PMID 11675511.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  18. ^ Scheer JM, Pearce G, Ryan CA (July 2005). "LeRALF, a plant peptide that regulates root growth and development, specifically binds to 25 and 120 kDa cell surface membrane proteins of Lycopersicon peruvianum". Planta. 221 (5): 667–74. doi:10.1007/s00425-004-1442-z. PMID 15909150.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  19. ^ Schopfer CR, Nasrallah ME, Nasrallah JB (November 1999). "The male determinant of self-incompatibility in Brassica". Science. 286 (5445): 1697–700. doi:10.1126/science.286.5445.1697. PMID 10576728.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  20. ^ Suzuki G, Kai N, Hirose T, et al. (September 1999). "Genomic organization of the S locus: Identification and characterization of genes in SLG/SRK region of S(9) haplotype of Brassica campestris (syn. rapa)". Genetics. 153 (1): 391–400. PMC 1460755. PMID 10471721.
  21. ^ Takayama S, Shiba H, Iwano M, et al. (February 2000). "The pollen determinant of self-incompatibility in Brassica campestris". Proc. Natl. Acad. Sci. U.S.A. 97 (4): 1920–5. doi:10.1073/pnas.040556397. PMC 26537. PMID 10677556.
  22. ^ Takayama S, Shimosato H, Shiba H, et al. (October 2001). "Direct ligand-receptor complex interaction controls Brassica self-incompatibility". Nature. 413 (6855): 534–8. doi:10.1038/35097104. PMID 11586363.
  23. ^ Kachroo A, Schopfer CR, Nasrallah ME, Nasrallah JB (September 2001). "Allele-specific receptor-ligand interactions in Brassica self-incompatibility". Science. 293 (5536): 1824–6. doi:10.1126/science.1062509. PMID 11546871.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  24. ^ Narita NN, Moore S, Horiguchi G, et al. (May 2004). "Overexpression of a novel small peptide ROTUNDIFOLIA4 decreases cell proliferation and alters leaf shape in Arabidopsis thaliana". Plant J. 38 (4): 699–713. doi:10.1111/j.1365-313X.2004.02078.x. PMID 15125775.
  25. ^ Wen J, Lease KA, Walker JC (March 2004). "DVL, a novel class of small polypeptides: overexpression alters Arabidopsis development". Plant J. 37 (5): 668–77. doi:10.1111/j.1365-313x.2003.01994.x. PMID 14871303.{{cite journal}}: CS1 maint: multiple names: authors list (link)
  26. ^ Butenko MA, Patterson SE, Grini PE, et al. (October 2003). "Inflorescence deficient in abscission controls floral organ abscission in Arabidopsis and identifies a novel family of putative ligands in plants". Plant Cell. 15 (10): 2296–307. doi:10.1105/tpc.014365. PMC 197296. PMID 12972671.
  27. ^ Jinn TL, Stone JM, Walker JC (January 2000). "HAESA, an Arabidopsis leucine-rich repeat receptor kinase, controls floral organ abscission". Genes Dev. 14 (1): 108–17. PMC 316334. PMID 10640280.{{cite journal}}: CS1 maint: multiple names: authors list (link)
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