期刊文献+

The cytosolic isoform of triosephosphate isomerase,ZmTPI4,is required for kernel development and starch synthesis in maize(Zea mays L.)

下载PDF
导出
摘要 Triosephosphate isomerase(TPI)is an enzyme that functions in plant energy production,accumulation,and conversion.To understand its function in maize,we characterized a maize TPI mutant,zmtpi4.In comparison to the wild type,zmtpi4 mutants showed altered ear development,reduced kernel weight and starch content,modified starch granule morphology,and altered amylose and amylopectin content.Protein,ATP,and pyruvate contents were reduced,indicating ZmTPI4 was involved in glycolysis.Although subcellular localization confirmed ZmTPI4 as a cytosolic rather than a plastid isoform of TPI,the zmtpi4 mutant showed reduced leaf size and chlorophyll content.Overexpression of ZmTPI4 in Arabidopsis led to enlarged leaves and increased seed weight,suggesting a positive regulatory role of ZmTPI4 in kernel weight and starch content.We conclude that ZmTPI4 functions in maize kernel development,starch synthesis,glycolysis,and photosynthesis.
出处 《The Crop Journal》 SCIE CSCD 2024年第2期401-410,共10页 作物学报(英文版)
基金 supported by the Major Public Welfare Projects of Henan Province(201300111100 to Yuling Li) Zhongyuan Scholars in Henan Province(22400510003 to Yuling Li) Tackle Program of Agricultural Seed in Henan Province(2022010201 to Yuling Li) Technical System of Maize Industry in Henan Province(HARS-2202-S to Yuling Li) State Key Laboratory of Wheat and Maize Crop Science(SKL2023ZZ05)。
  • 相关文献

参考文献4

二级参考文献111

  • 1Aparicio, R., Ferreira, S.T., and Polikarpov, I. (2003). Closed conformation of the active site loop of rabbit muscle triosephosphate isomerase in the absence of substrate: evidence of conformational heterogeneity. J. Mol. Biol. 334,1023-1041.
  • 2Astier, J., Rasul, 5., Koen, E., Manzoor, H., Besson-Bard, A., Lamotte, 0., Jeandroz, 5., Durner, J., Lindermayr. c.. and Wendehenne, D. (2011). S-nitrosylation: an emerging post-translational protein modification in plants. Plant Sci. 181, 527-533.
  • 3Balmer, Y., Koller, A., del Val, G., Manieri, W., Schurmann, p', and Buchanan, B.B. (2003). Proteomics gives insight into the regulatory function of chloroplast thioredoxins. Proc. Natl Acad. Sci. USA. 100, 370-375.
  • 4Banner, D.W., Bloomer, A.c., Petsko, G.A., Phillips, D.C., Pogson, C.I., Wilson, I.A., Corran, P.H., Furth, A.J., Milman, J.D., Offord, R.E., et al, (1975). Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. Nature. 255, 609-614.
  • 5Bedhomme, M., Adamo, M., Marchand, C.H., Couturier, J., Rouhier, N., Lemaire, S.D., Zaffagnini, M., and Trost, P. (2012). Glutathionylation of cytosolic glyceraldehyde-3-phosphate dehydrogenase from the model plant Arabidopsis thaliana is reversed by both glutaredoxins and thioredoxins in vitro. Biochem. J. 445,337-347.
  • 6Bedhomme, M., Zaffagnini, M., Marchand, C.H., Gao, X.H., Moslonka-Lefebvre, M., Michelet, L., Decottignies, p', and Lemaire, S.D. (2009). Regulation by glutathionylation of isocitrate lyase from Chlamydomonas reinhardtii. J. Biol. Chem. 284, 36282-36291.
  • 7Benhar. M . Forrester. M.T . and Stamler. J.S. (2009). Protein denitrosylation: enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 10, 721-732.
  • 8Benhar. M., Thompson. J.W . Moseley. M.A., and Stamler, J.S. (2010). Identification of S-nitrosylated targets of thioredoxin using a quantitative proteomic approach. Biochemistry. 49, 6963-6969.
  • 9Besson-Bard, A . Pugin, A., and Wendehenne, D. (2008). New insights into nitric oxide signaling in plants. Annu. Rev. Plant Biol. 59, 21-39.
  • 10Borchert. T.V., Pratt, K . Zeelen. J.P', Callens, M . Noble, M.E., Opperdoes, F.R., Michels, P.A . and Wierenga, R.K. (1993). Overexpression of trypanosoma I triosephosphate isomerase in Escherichia coli and characterisation of a dimer-interface mutant. Eur. J. Biochem. 211, 703-710.

共引文献21

相关作者

内容加载中请稍等...

相关机构

内容加载中请稍等...

相关主题

内容加载中请稍等...

浏览历史

内容加载中请稍等...
;
使用帮助 返回顶部