Annexins and their role in the control of symbioses development in plants

Cover Page


Cite item

Full Text

Open Access Open Access
Restricted Access Access granted
Restricted Access Subscription or Fee Access

Abstract

Annexins belong to the superfamily of calcium-dependent phospholipid binding proteins. The participation of these proteins in the regulation of structural organization of membranes, vesicular transport and a variety of signal transduction pathways is important for many cellular processes. Despite the structural similarity with animal annexins, plant annexins are characterized by significant variability of the N-terminal region and modification of calcium-binding motifs in II and III repeats, while calcium-binding motifs in I and IV repetitions remain conservative. However, the physiological role of animal and plant annexins, as well as mechanisms of their influence on calcium metabolism, may be similar. This review focused on the latest data about the structure and functioning of plant annexins.

Full Text

Restricted Access

About the authors

Darya V. Kustova

Federal State Budget Scientific Institution All-Russia Research Institute for Agricultural Microbiology

Email: dasha_94-07@mail.ru

младший научный сотрудник

Russian Federation, Saint Petersburg

Elena A. Dolgikh

Federal State Budget Scientific Institution All-Russia Research Institute for Agricultural Microbiology

Author for correspondence.
Email: dol2helen@yahoo.com
ORCID iD: 0000-0002-5375-0943
SPIN-code: 4453-2060
Scopus Author ID: 6603496335
ResearcherId: G-6363-2017

Doctor of Sciences, Head, Laboratory of Signal Regulation

Russian Federation, Saint Petersburg

References

  1. Clark GB, Morgan RO, Fernandez MP, Roux SJ. Evolutionary adaptation of plant annexins has diversified their molecular structures, interactions and functional roles. New Phytol. 2012;196(3):695-712. https://doi.org/10.1111/j.1469-8137.2012.04308.x.
  2. Boustead CM, Smallwood M, Small H, et al. Identification of calcium-dependent phospholipid-binding proteins in higher plant cells. FEBS Lett. 1989;244(2):456-460. https://doi.org/10.1016/0014-5793(89)80582-4.
  3. Moss SE, Morgan RO. The annexins. Genome Biol. 2004;5(4):219. https://doi.org/10.1186/gb-2004-5-4-219.
  4. Gerke V, Moss SE. Annexins: From Structure to Function. Physiol Rev. 2002;82(2):331-371. https://doi.org/10.1152/physrev.00030.2001.
  5. Hu T, Shi J, Jiao X, et al. Measurement of annexin V uptake and lactadherin labeling for the quantification of apoptosis in adherent Tca8113 and ACC-2 cells. Brazilian J Med Biol Res. 2008;41(9):750-757. https://doi.org/10.1590/S0100-879X2008000900002.
  6. Konopka-Postupolska D, Clark G. Annexins as overlooked regulators of membrane trafficking in plant cells. Int J Mol Sci. 2017;18(4):863. https://doi.org/10.3390/ijms18040863.
  7. Mortimer JC, Laohavisit A, Macpherson N, et al. Annexins: multifunctional components of growth and adaptation. J Exp Bot. 2008;59(3):533-544. https://doi.org/10.1093/jxb/erm344.
  8. Clark GB, Rafati DS, Bolton RJ, et al. Redistribution of annexin in gravistimulated pea plumules. Plant Physiol Biochem. 2000;38(12):937-947. https://doi.org/10.1016/S0981-9428(00)01206-7.
  9. Breton G, Vazquez-Tello A, Danyluk J, Sarhan F. Two novel intrinsic annexins accumulate in wheat membranes in response to low temperature. Plant Cell Physiol. 2000;41(2):177-184. https://doi.org/10.1093/pcp/41.2.177.
  10. Kovacs I, Ayaydin F, Oberschall A, et al. Immunolocalization of a novel annexin-like protein encoded by a stress and abscisic acid responsive gene in alfalfa. Plant J. 1998;15(2):185-197. https://doi.org/10.1046/j.1365-313X.1998. 00194.x.
  11. Clark GB, Dauwalder M, Roux SJ. Immunological and biochemical evidence for nuclear localization of annexin in peas. Plant Physiol Biochem. 1998;36(9):621-627. https://doi.org/10.1016/S0981-9428(98)80010-7.
  12. Feng YM, Wei XK, Liao WX, et al. Molecular analysis of the annexin gene family in soybean. Biol Plant. 2013;57(4):655-662. https://doi.org/10.1007/s10535-013-0334-0.
  13. Davies J. Annexin-Mediated calcium signalling in plants. Plants (Basel). 2014;3(1):128-140. https://doi.org/10.3390/plants3010128.
  14. Laohavisit A, Richards SL, Shabala L, et al. Salinity-Induced calcium signaling and root adaptation in arabidopsis require the calcium regulatory protein annexin1. Plant Physiol. 2013;163(1):253-262. https://doi.org/10.1104/pp.113.217810.
  15. Kodavali PK, Skowronek K, Koszela-Piotrowska I, et al. Structural and functional characterization of annexin 1 from Medicago truncatula. Plant Physiol Biochem. 2013;73:56-62. https://doi.org/10.1016/j.plaphy.2013.08.010.
  16. Chung JS, Zhu JK, Bressan RA, et al. Reactive oxygen species mediate Na+-induced SOS1 mRNA stability in Arabidopsis. Plant J. 2008;53(3):554-565. https://doi.org/10.1111/j.1365-313X.2007.03364.x.
  17. Carrasco-Castilla J, Ortega-Ortega Y, Jáuregui-Zúñiga D, et al. Down-regulation of a Phaseolus vulgaris annexin impairs rhizobial infection and nodulation. Environ Exp Bot. 2018;153: 108-119. https://doi.org/10.1016/j.envexpbot. 2018.05.016.
  18. Talukdar T, Gorecka KM, de Carvalho-Niebel F, et al. Annexins-calcium- and membrane-binding proteins in the plant kingdom. Potential role in nodulation and mycorrhization in Medicago truncatula. Acta Biochim Pol. 2009;56(2): 199-210.
  19. De Carvalho Niebel F, Lescure N, Cullimore JV, Gamas P. The Medicago truncatula MtAnn1 gene encoding an annexin is induced by nod factors and during the symbiotic interaction with Rhizobium meliloti. Mol Plant Microbe Interact. 1998;11(6):504-513. https://doi.org/10.1094/MPMI.1998.11.6.504.
  20. De Carvalho-Niebel F, Timmers AC, Chabaud M, et al. The Nod factor-elicited annexin MtAnn1 is preferentially localised at the nuclear periphery in symbiotically activated root tissues of Medicago truncatula. Plant J. 2002;32(3):343-352. https://doi.org/10.1046/j.1365-313x.2002.01429.x.
  21. Glyan’ko AK. Physiological role of signal systems in the formation of legume-rhizobial symbiosis. J Agric Environ. 2018;3(7):1-15. http://dx.doi.org/10.23649/jae.2018.3.7.2.
  22. Lefebvre B, Furt F, Hartmann MA, et al. Characterization of lipid rafts from Medicago Truncatula root plasma membranes: a proteomic study reveals the presence of a raft-associated redox system. Plant Physiol. 2007;144(1):402-418. https://doi.org/10.1104/pp.106.094102.
  23. Nguyen TH, Brechenmacher L, Aldrich JT, et al. Quantitative phosphoproteomic analysis of soybean root hairs inoculated with Bradyrhizobium japonicum. Mol Cell Proteomics. 2012;11(11):1140-1155. https://doi.org/10.1074/mcp.M112.018028.
  24. Manthey K, Krajinski F, Hohnjec N, et al. Transcriptome profiling in root nodules and arbuscular mycorrhiza identifies a collection of novel genes induced during Medicago Truncatula root endosymbioses. Mol Plant Microbe Interact. 2004;17(10):1063-1077. https://doi.org/10.1094/MPMI.2004.17.10.1063.
  25. Amiour N, Recorbet G, Robert F, et al. Mutations in DMI3 and SUNN modify the appressorium-responsive root proteome in arbuscular mycorrhiza. Mol Plant Microbe Interact. 2006;19(9):988-997. https://doi.org/10.1094/MPMI-19-0988.
  26. Deguchi Y, Banba M, Shimoda Y, et al. Transcriptome profiling of lotus japonicus roots during arbuscular mycorrhiza development and comparison with that of nodulation. DNA Res. 2007;14(3):117-133. https://doi.org/10.1093/dnares/dsm014.
  27. Handa Y, Nishide H, Takeda N, et al. RNA-seq Transcriptional profiling of an arbuscular mycorrhiza provides insights into regulated and coordinated gene expression in Lotus japonicus and Rhizophagus irregularis. Plant Cell Physiol. 2015;56(8):1490-1511. https://doi.org/10.1093/pcp/pcv071.

Supplementary files

Supplementary Files
Action
1. JATS XML
Download
2. Figure: 1. Comparative analysis of amino acid sequences of two Medicago truncatula annexins MtAnn1 (NCBI CAD29698.1), MtAnn2 (NCBI AES68900.1), and two annexins Phaseolus vulgaris PvAnn1 (NCBI Phvul.011G209300.1), PvAnn2 (NCBI Phvul.1.0) ... The four annexin repeats are underlined and marked with Roman numerals I – IV. Potential calcium-binding motifs are highlighted in gray. In the first annexin repeat, conserved tryptophan is noted, which is necessary for binding to the membrane

Download (328KB)
Indexing metadata
3. Figure: 2. The spatial structure of the M. truncatula annexin MtAnn2 was constructed using the Modeller 9.20 program. using cotton Gossypium hirsutum (PDB code P93157) as a template for annexin GhAnn1 3D structure. The structure was visualized using the PyMol program

Download (349KB)
Indexing metadata

Copyright (c) 2020 Kustova D.V., Dolgikh E.A.

Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
СМИ зарегистрировано Федеральной службой по надзору в сфере связи, информационных технологий и массовых коммуникаций (Роскомнадзор).
Регистрационный номер и дата принятия решения о регистрации СМИ: серия ПИ № ФС 77 - 65617 от 04.05.2016.


This website uses cookies

You consent to our cookies if you continue to use our website.

About Cookies