Functional Analysis of PH-START1 in Regulating Growth and Development of Arabidopsis thaliana

doi:10.7668/hbnxb.201751132

Abstract

Abstract: In order to clarify the function of PH-START1 (At2g28320) in regulating the growth and development of Arabidopsis, the expression of PH-START1 in different organs of Arabidopsis during different growth periods was analyzed by Real-time PCR, and the space-time expression characteristics of PH-START1 was determined. The PH-START1 function-obtaining and function-missing transgenic Arabidopsis were created and their phenotypes were analyzed. The biological function of PH-START1 in regulating the growth and development of Arabidopsis was elucidated. The Real-time PCR results showed that the expression of PH-START1 gene presented in the roots, leaves, flowers and siliques, and the highest expression level of PH-START1 was found in roots at seedling stage. The highest expression of the gene was in the 6th rosette leaf, then gradually decreased as the development time extended. In the development period of flowers, the expression of PH-START1 increased gradually with the development time of flowers. The highest expression of PH-START1 in kernels presented in 3-5 d after pollination, and then gradually decreased, but the expression of PH-START1 increased slightly in 9 d kernels after pollination. The highest expression of PH-START1 was in stamens, followed by petals and sepals, and the least in pistil. In order to analyze the function of PH-START1 in regulating the growth and development of Arabidopsis, the phenotype of the gain-of-function (overexpression, OE) and deletion (T-DNA insertion, ph-start1) transgenic Arabidopsis of PH-START1 was observed. The vegetative growth of PH-START1 overexpressing Arabidopsis was significantly inhibited, presenting shorter plant, weaker stems, smaller leaves and less roots. This suggested that PH-STARTI had a negative regulatory role in the growth and development of Arabidopsis, which provided a theoretical basis for elucidating and promoting the plant growth and development.

Key words: PH-START1, Arabidopsis thaliana, Growth and development, Real-time PCR

CLC Number:

Q945.49

ZHAO Yazhuo, WANG Xin, FENG Jiajia, SUN Dandan, WANG Fengru, DONG Jingao. Functional Analysis of PH-START1 in Regulating Growth and Development of Arabidopsis thaliana[J]. ACTA AGRICULTURAE BOREALI-SINICA, 2019, 34(2): 87-94. doi: 10.7668/hbnxb.201751132.

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References

[1] Ogawa E, Yamada Y, Sezaki N, Kosaka S A, Kamata N, Abe M, Komeda Y, Takahashi T. ATML1 and PDF2 play a redundant and essential role in Arabidopsis embryo development[J].Plant and Cell Physiology,2015,56(6):1183-1192.doi:10.1093/pcp/pcv045.
[2] Rombola-Caldentey B, Rueda-Romero P A, Carbonero P, Onate-Sanchez L. Arabidopsis DELLA and two HD-ZIP transcription factors regulate GA signaling in the epidermis through the L1 box cis-Element[J].Plant Cell,2014,26(7):2905-2919.doi:10.1105/tpc.114.127647.
[3] Zhu Y, Rong L, Luo Q, Wang B H, Zhou N A, Yang Y E, Zhang C, Feng H Y, Zheng L A, Shen W H, Ma J B, Dong A W. The histone chaperone NRP1 interacts with WEREWOLF to activate GLABRA2 in Arabidopsis root hair development[J].Plant Cell,2017,29(2):260-276.doi:10.1105/tpc.16.00719.
[4] Schrick K, Nguyen D, Karlowski W M, Mayer K F. START lipid/sterol-binding domains are amplified in plants and are predominantly associated with homeodomain transcription factors[J].Genome Biology,2004,5(6):R41.doi:10.1186/gb-2004-5-6-r41.
[5] Tang D Z, Ade J, Frye C A, Innes R W. Regulation of plant defense responses in Arabidopsis by EDR2, a PH and START domain-containing protein[J].Plant Journal,2005,44(2):245-257.doi:10.1111/j.1365-313X.2005.02523.x.
[6] Shaw G.Identification of novel pleckstrin homology(PH)domains provides a hypothesis for PH domain function[J].Biochemical and Biophysical Research Communications, 1993, 195(2):1145-1151.doi:10.1006/bbrc.1993.2164.
[7] Sneha R, Pallavi M, Modeling S B. Dynamics and phosphoinositide binding of the pleckstrin homology domain of two novel PLCs:η1 and η2[J].Journal of Molecular Graphics & Modelling,2018(85):130-144.doi:10.1016/j.jmgm.2018.07.012.
[8] Kang Y L, Kim B G, Kim S, Lee Y A.Inhibitory potential of flavonoids on Ptdlns(3,4,5)P3 binding with the phosphoinositide-dependent kinase 1 pleckstrin homology domain[J].Bioorganic & Medicinal Chemistry Letters,2017,27(3):420-426.doi:10.1016/j.bmc1.2016.12.051.
[9] Rebecchi M J, Scarlata S.Pleckstrin homology domains:A common fold with diverse functions[J].Annual Review of Biophysics and Biomolecular Structure,1998,27(4):503.doi:10.1146/annurev.biophys.27.1.503.
[10] Naughton F B, Kalli A C, Sansom M S. Modes of interaction of pleckstrin homology domains with membranes:toward a computational biochemistry of membrane recognition[J].Journal of Molecular Biology,2018,430(3):372-388.doi:10.1016/j.jmb.2017.12.011.
[11] Kalli A C, Campbell I D, Sansom M S. Interactions of the kindlin family pleckstrin homology domains with model membranes containing zwitterionic lipids and phosphatidyl inositol phosphates[J].Biophysical Journal,2014,106(2, 1):517A.doi:10.1016/j.bpj.2013.11.2889.
[12] Goraia S, Bagdia P R, Boraha R, Paulb D, Santrab M K, Khanc A T, Mannaa D. Insights into the inhibitory mechanism of triazole-based small molecules on phosphatidylinositol-4,5-bisphosphate binding pleckstrin homology domain[J].Biochemistry and Biophysics Reports, 2015, 2:75-86.doi:10.1016/j.bbrep.2015.05.007.
[13] Panda P K, Behera B, Meher B R, Mukhopadhyay S, Sinha N A, Roy B, Das J, Paul S, Maiti T K, Agarwal R, Bhutia S K. Abrus agglutinin, a type Ⅱ ribosome inactivating protein inhibits Akt/PH domain to induce endoplasmic reticulum stress mediated autophagy-dependent cell death[J].Molecular Carcinogenesis,2017,56(2):389-401.doi:10.1002/mc.22502.
[14] Lemmon M A.Phosphoinositide recognition domains[J].Traffic,2003,4(4):201-213.doi:10.1034/j.1600-0854.2004.00071.x.
[15] Kumagai K, Elwell C A, Ando S, Engel J N, Hanada K.Both the N-and C-terminal regions of the Chlamydial inclusion protein D (IncD) are required for interaction with the pleckstrin homology domain of the ceramide transport protein CERT[J].Biochemical and Biophysical Research Communications,2018,505(4):1070-1076.doi:10.1016/j.bbrc.2018.09.168.
[16] 周苹. GH3.9 基因过表达对拟南芥生长发育的影响研究[D]. 长沙:湖南大学, 2013.doi:10.7666/d.Y2523085.
Zhou P. Effect of over-expression og GH3.9 gene on the plant growth and development of Arabidopsis[D]. Changsha:Hunan University, 2013.
[17] Romanowski M J, Soccio R E, Breslow J L, Burley S K.Crystal structure of the Mus musculus cholesterol-regulated START protein 4(StarD4) containing a StAR-related lipid transfer domain[J].Proceedings of the National Academy of Sciences of the United States of America,2002,99(10):6949-6954.doi:10.1073/pnas.052140699.
[18] Kang Y, Jang G, Ahn S, Lee Y A, Yoon Y. Regulation of AKT activity by inhibition of the pleckstrin homology Doniam-PtdIns(3,4,5)P-3 interaction using flavonoids[J].Journal of Microbiology and Biotechnology,2018,28(8):1401-1411.doi:10.4014/jmb.1804.04051.
[19] Yamada S, Yamaguchi T, Hosoda A, Iwawaki T, Kohno K. Regulation of human STARD4 gene expression under endoplasmic reticulum stress[J].Biochemical and Biophysical Research Communications,2006,343(4):1079-1085.doi:10.1016/j.bbrc.2006.03.051.
[20] Sluchanko N N, Tugaeva K V, Maksimov E G.Solution structure of human steroidogenic acute regulatory protein STARD1 studied by small-angle X-ray scattering[J].Biochemical and Biophysical Research Communications,2017,489(4):445-450.doi:10.1016/j.bbrc.2017.05.167.
[21] Kubo H, Peeters A J, Aarts M G, Pereira A, Koornneef M.ANTHOCYANINLESS2, a homeobox gene affecting anthocyanin distribution and root development in Arabidopsis[J].The Plant Cell,1999,11(7):1217-1226.doi:10.2307/3870744.
[22] Schrick K, Bruno M, Khosla A, Cox P N, Marlatt S A, Roque R A, Nguyen H C, Snyder M P, Singh D, Yadav G.Shared functions of plant and mammalian StAR-related lipid transfer (START) domains in modulating transcription factor activity[J].BMC Biology,2014,12:70-78.doi:10.1186/s12915-014-0070-8.

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