Характеристика нового гена монодегидроаскорбатредуктазы у кукурузы (Zea mays L.) и его роль в ответе на стрессы

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Abstract

Растения кукурузы Zea mays L. чувствительны ко многим стрессовым факторам, вызывающим избыточное образование активных форм кислорода, механизм нивелирования воздействия которых на организм включает фермент монодегидроаскорбатредуктазу (MDHAR; EC 1.6.5.4), катализирующий восстановление монодегидроаскорбиновой кислоты до аскорбата. В геноме кукурузы известно четыре гена ZmMDHAR1–ZmMDHAR4, различающихся внутриклеточной локализацией кодируемых белков MDHAR. В данной работе был идентифицирован новый ген семейства – ZmMDHAR5 (Zm00001d017786; LOC100193942), кодирующий близкий структурный гомолог пероксисомального ZmMDHAR3. Сделано предположение, что ZmMDHAR5 может иметь функции, близкие к хлоропласт-митохондриальным MDHAR. Дифференциальная экспрессия генов ZmMDHAR1–ZmMDHAR5 в проростках кукурузы в ответ на различные стрессовые факторы позволила также предположить важное участие ZmMDHAR4 и ZmMDHAR5 в ответе на экзогенную абсцизовую кислоту, низкие температуры и обезвоживание; ZmMDHAR1 и ZmMDHAR3 – на солевой стресс; ZmMDHAR2 – на избыток соли и дефицит воды.

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М. А. Филюшин

Федеральный исследовательский центр “Фундаментальные основы биотехнологии” Российской академии наук

Author for correspondence.
Email: michel7753@mail.ru

Институт биоинженерии

Russian Federation, Москва

Д. Х. Архестова

Федеральный исследовательский центр “Фундаментальные основы биотехнологии” Российской академии наук; Федеральный научный центр “Кабардино-Балкарский научный центр Российской академии наук”

Email: michel7753@mail.ru

Институт биоинженерии, Институт сельского хозяйства

Russian Federation, Москва; Нальчик

Е. З. Кочиева

Федеральный исследовательский центр “Фундаментальные основы биотехнологии” Российской академии наук

Email: michel7753@mail.ru

Институт биоинженерии

Russian Federation, Москва

А. В. Щенникова

Федеральный исследовательский центр “Фундаментальные основы биотехнологии” Российской академии наук

Email: michel7753@mail.ru

Институт биоинженерии

Russian Federation, Москва

References

  1. Gill S.S., Tuteja N. Reactive oxygen species and antioxidant machinery in abiotic stress tolerance in crop plants // Plant Physiol. Biochem. 2010. V. 48. P. 909. https://doi.org/10.1016/j.plaphy.2010.08.016
  2. Mittler R. Oxidative stress, antioxidants and stress tolerance // Trends Plant Sci. 2002. V. 7. P. 405.
  3. Smirnoff N. Ascorbic acid metabolism and functions: A comparison of plants and mammals // Free Radic. Biol. Med. 2018. V. 22. P. 116. https://doi.org/10.1016/j.freeradbiomed.2018.03.033
  4. Leterrier M., Corpas F.J., Barroso J.B., Sandalio L.M., del Río L.A. Peroxisomal monodehydroascorbate reductase, genomic clone characterization and functional analysis under environmental stress conditions // Plant Physiol. 2005. V. 138. P. 2111. https://doi.org/10.1104/pp.105.066225
  5. Sano S., Tao S., Endo Y., Inaba T., Hossain M.A., Miyake C., Matsuo M., Aoki H., Asada K., Saito K. Purification and cDNA cloning of chloroplastic monodehydroascorbate reductase from spinach // Biosc. Biotechnol. Biochem. 2005. V. 69. P. 762.
  6. Zhou F., Zheng B., Wang F., Cao A., Xie S., Chen X., Schick J.A., Jin X., Li H. Genome-Wide Analysis of MDHAR gene family in four cotton species provides insights into fiber development via regulating AsA redox homeostasis // Plants. 2021. V. 10. Article 227. https://doi.org/10.3390/plants10020227
  7. Feng H., Liu W., Zhang Q., Wang X., Wang X., Duan X., Li F., Huang L., Kang Z. TaMDHAR4, a monodehydroascorbate reductase gene participates in the interactions between wheat and Puccinia striiformis f. sp. tritici // Plant Physiol. Biochem. 2014. V. 76. P. 7. https://doi.org/10.1016/j.plaphy.2013.12.015
  8. Lanubile A., Maschietto V., De Leonardis S., Battilani P., Paciolla C., Marocco A. Defense responses to mycotoxin-producing fungi Fusarium proliferatum, F. subglutinans, and Aspergillus flavus in kernels of susceptible and resistant maize genotypes // Mol. Plant Microbe Interact. 2015. V. 28. P. 546. https://doi.org/10.1094/MPMI-09-14-0269-R
  9. Negi B., Salvi P., Bhatt D., Majee M., Arora S. Molecular cloning, in-silico characterization and functional validation of monodehydroascorbate reductase gene in Eleusine coracana // PLoS ONE. 2017. V. 12. Article e0187793. https://doi.org/10.1371/journal.pone.0187793
  10. Zhang Y., Li Z., Peng Y., Wang X., Peng D., Li Y., He X., Zhang X., Ma X., Huang L., Yan Y. Clones of FeSOD, MDHAR, DHAR Genes from white clover and gene expression analysis of ROS-scavenging enzymes during abiotic stress and hormone treatments // Molecules. 2015. V. 20. P. 20939. https://doi.org/10.3390/molecules201119741
  11. García G., Clemente-Moreno M.J., Díaz-Vivancos P., García M., Hernández J.A. The apoplastic and symplastic antioxidant system in onion: response to long-term salt stress // Antioxidants. 2020. V. 12. Article 67. https://doi.org/10.3390/antiox9010067
  12. Qi Q., Yanyan D., Yuanlin L., Kunzhi L., Huini X., Xudong S. Overexpression of SlMDHAR in transgenic tobacco increased salt stress tolerance involving S-nitrosylation regulation // Plant Sci. 2020. V. 299. Article 110609. https://doi.org/10.1016/j.plantsci.2020.110609
  13. Sultana S., Khew C.Y., Morshed M.M., Namasivayam P., Napis S., Ho C.L. Overexpression of monodehydroascorbate reductase from a mangrove plant (AeMDHAR) confers salt tolerance on rice // J. Plant Physiol. 2012. V. 169. P. 311. https://doi.org/10.1016/j.jplph.2011.09.004
  14. Liu Y.J., Yuan Y., Liu Y.Y., Liu Y., Fu J.J., Zheng J., Wang G.Y. Gene families of maize glutathione-ascorbate redox cycle respond differently to abiotic stresses // J. Plant Physiol. 2012. V. 169. P. 183. https://doi.org/10.1016/j.jplph.2011.08.018
  15. Sanahuja G., Farré G., Bassie L., Zhu C., Christou P., Capell T. Ascorbic acid synthesis and metabolism in maize are subject to complex and genotype-dependent feedback regulation during endosperm development // Biotechnol. J. 2013. V. 8. P. 1221. https://doi.org/10.1002/biot.201300064
  16. Sytykiewicz H. Expression patterns of genes involved in ascorbate-glutathione cycle in aphid-infested maize (Zea mays L.) seedlings // Int. J. Mol. Sci. 2016. V. 17. Article 268. https://doi.org/10.3390/ijms17030268
  17. Hu X., Liu J., Li W., Wen T., Li T., Guo X., Liu R.H. Biosynthesis and accumulation of multi-vitamins in black sweet corn (Zea mays L.) during kernel development // J. Sci. Food Agric. 2020. V. 100. P. 5230. https://doi.org/10.1002/jsfa.10573
  18. Filyushin M.A., Kochieva E.Z., Shchennikova A.V. ZmDREB2.9 gene in maize (Zea mays L.): genome-wide identification, characterization, expression, and stress response // Plants. 2022. V. 11. P.3060. https://doi.org/10.3390/plants11223060
  19. Liu J., Sun X., Xu F., Zhang Y., Zhang Q., Miao R., Zhang J., Liang J., Xu W. Suppression of OsMDHAR4 enhances heat tolerance by mediating H2O2-induced stomatal closure in rice plants // Rice. 2018. V. 11. Article 38. https://doi.org/10.1186/s12284-018-0230-5
  20. Yoon H.S., Lee H., Lee I.A., Kim K.Y., Jo J. Molecular cloning of the monodehydroascorbate reductase gene from Brassica campestris and analysis of its mRNA level in response to oxidative stress // Biochim. Biophys. Acta. 2004. V. 1658. P. 181. https://doi.org/10.1016/j.bbabio.2004.05.013
  21. Chen Q., Li W., Tan L., Tian F. Harnessing knowledge from maize and rice domestication for new crop breeding // Mol. Plant. 2021. V. 14. P. 9. https://doi.org/10.1016/j.molp.2020.12.006
  22. Zhou X., Muhammad I., Lan H., Xia C. Recent advances in the analysis of cold tolerance in maize // Front Plant Sci. 2022. V. 13. Article 866034. https://doi.org/10.3389/fpls.2022.866034
  23. Xie T., Gu W., Zhang L., Li L., Qu D., Li C., Meng Y., Li J., Wei S., Li W. Modulating the antioxidant system by exogenous 2-(3,4-dichlorophenoxy) triethylamine in maize seedlings exposed to polyethylene glycol-simulated drought stress // PLoS One. 2018. V. 13. Article e0203626. https://doi.org/10.1371/journal.pone.0203626
  24. Omoto E., Nagao H., Taniguchi M., Miyake H. Localization of reactive oxygen species and change of antioxidant capacities in mesophyll and bundle sheath chloroplasts of maize under salinity // Physiol. Plant. 2013. V. 149. P. 1. https://doi.org/10.1111/ppl.12017
  25. Bryła M., Pierzgalski A., Zapaśnik A., Uwineza P.A., Ksieniewicz-Woźniak E., Modrzewska M., Waśkiewicz A. Recent research on Fusarium mycotoxins in maize-a review // Foods. 2022. V. 11. Article 3465. https://doi.org/10.3390/foods11213465
  26. Ismaiel A.A., Papenbrock J. Effect of patulin from Penicillium vulpinum on the activity of glutathione-s-transferase and selected antioxidative enzymes in maize // Int. J. Environ. Res. Public Health. 2017. V. 14. Article 825. https://doi.org/10.3390/ijerph14070825
  27. Shabeer S., Asad S., Jamal A., Ali A. Aflatoxin contamination, its impact and management strategies: an updated review // Toxins. 2022. V. 14. Article 307. https://doi.org/10.3390/toxins14050307
  28. Wang J., Zhong X., Zhu K., Lv J., Lv X., Li F., Shi Z. Reactive oxygen species, antioxidant enzyme activity, and gene expression patterns in a pair of nearly isogenic lines of nicosulfuron-exposed waxy maize (Zea mays L.) // Environ. Sci. Pollut. Res. Int. 2018. V. 25. P. 19012. https://doi.org/10.1007/s11356-018-2105-0
  29. Lisenbee C.S., Lingard M.J., Trelease R.N. Arabidopsis peroxisomes possess functionally redundant membrane and matrix isoforms of monodehydroascorbate reductase // Plant J. 2005. V. 43. P. 900. https://doi.org/10.1111/j.1365-313X.2005.02503.x
  30. Hu B., Zeng W.P., Li X., Al-Sheikh U., Chen S.Y., Ding J. A conserved arginine/lysine-based motif promotes ER export of KCNE1 and KCNE2 to regulate KCNQ1 channel activity // Channels. 2019. V. 13. P. 483. https://doi.org/10.1080/19336950.2019.1685626
  31. Kano T., Kouzuki T., Mizuno S., Ueda S., Yamanoue M., Sakane F., Saito N., Shirai Y. Both the C1 domain and a basic amino acid cluster at the C-terminus are important for the neurite and branch induction ability of DGKβ // Biochem. Biophys. Res. Commun. 2014. V. 447. P. 89. https://doi.org/10.1016/j.bbrc.2014.03.113
  32. Lunde C., Baumann U., Shirley N.J., Drew D.P., Fincher G.B. Gene structure and expression pattern analysis of three monodehydroascorbate reductase (Mdhar) genes in Physcomitrella patens: implications for the evolution of the MDHAR family in plants // Plant Mol. Biol. 2006. V. 60. P. 259. https://doi.org/10.1007/s11103-005-3881-8
  33. De Vleesschauwer D., Xu J., Höfte M. Making sense of hormone-mediated defense networking: from rice to Arabidopsis // Front. Plant Sci. 2014. V. 5. Article 611. https://doi.org/10.3389/fpls.2014.00611
  34. Huang B., Zhang J.M., Chen X.L., Xin X., Yin G.K., He J.J., Lu X.X., Zhou Y.C. Oxidative damage and antioxidative indicators in 48 h germinated rice embryos during the vitrification-cryopreservation procedure // Plant Cell Rep. 2018. V. 37. P. 1325. https://doi.org/10.1007/s00299-018-2315-4
  35. Koffler B.E., Luschin-Ebengreuth N., Stabentheiner E., Müller M., Zechmann B. Compartment specific response of antioxidants to drought stress in Arabidopsis // Plant Sci. 2014. V. 227. P. 133. https://doi.org/10.1016/j.plantsci.2014.08.002
  36. Fenech M., Amaya I., Valpuesta V., Botella M.A. Vitamin C content in fruits: biosynthesis and regulation // Front. Plant Sci. 2019. V. 9. Article 2006. https://doi.org/10.3389/fpls.2018.02006

Supplementary files

Supplementary Files
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1. JATS XML
2. Fig. 1. Variants (1-4) of the ZmMDHAR3–ZmMDHAR5 fragment on chromosome 5 in the genome of 35 maize samples, including the exon-intron structure of the ZmMDHAR3 genes (exons are indicated by blue blocks) and ZmMDHAR5 (exons are indicated by pink blocks); the red line indicates the intergenic spacer.

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3. Fig. 2. Alignment of sequences of proteins of the ZmMDHAR family. The Pyr_redox_2 domain (pfam07992) is underlined in red. The binding sites with FAD/NAD(P)H cofactors are highlighted in black. The consensus GxGxxG/GxGxxxG is highlighted in blue.

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4. Fig. 3. a is a phylogenetic tree based on sequences of MDHARs proteins of rice O. sativa (OsMDHAR1 (NP_001404045.1), OsMDHAR2 (NP_001403773.1), OsMDHAR3 (XP_015611766.1), OsMDHAR4 (NP_001390619.1), OsMDHAR5 (XP_015649952.1)), Asparagus As. officinalis (AoMDHAR1 (XP_020260315.1), AoMDHAR4 (XP_020251572.1), AoMDHAR5 (XP_020241046.1)), garlic A. sativum (AsMDHAR1 (Asa7G02482.1), AsMDHAR4 (Asa0G05211.1), AsMDHAR5 (Asa5G00445.1)), A. thaliana (AtMDHAR1 (At3g52880, NP_190856), AtMDHAR2 (At5g03630, NP_568125.1), AtMDHAR3 (At3g09940, NP_566361.1), AtMDHAR4 (At3g27820, NP_189420.1), AtMDHAR6 (At1g63940, NP_849839.1)) and P. patens ( PpMDHAR1 (ABA47446.1), PpMDHAR2 (ABA47447.1) and PpMDHAR3 (ABA47448.1)). The dendrogram was built using the MEGA 7.0 program (Maximum Likelihood method, 1000 bootstrap replicas). b – Conservative motifs identified using MEME 5.1.1 in MDHAR proteins.

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5. Fig. 4. Differential expression of ZmMDHAR genes in response to treatment with ABA (100 microns), cold stress (+3°C), salt stress (NaCl, 250 mM) and dehydration (10% PEG-6000) for 6 and 24 hours. The raw control is accepted as 1.

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6. Supplementary information
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Note

1 Дополнительные материалы размещены в электронном виде по DOI статьи: 10.31857/S0015330324010067


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