RLIN1, encoding a putative coproporphyrinogen III oxidase, is involved in lesion initiation in rice

Changhui Sun; Linchuan Liu; Jiuyou Tang; Aihong Lin; Fantao Zhang; Jun Fang; Genfa Zhang; Chengcai Chu

doi:10.1016/j.jcg.2010.12.001

Volume 38 Issue 1

Jan. 2011

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RLIN1, encoding a putative coproporphyrinogen III oxidase, is involved in lesion initiation in rice

doi: 10.1016/j.jcg.2010.12.001

Changhui Sun^{a, b, d, #},
Linchuan Liu^{b, c, #},
Jiuyou Tang^b,
Aihong Lin^{b, c},
Fantao Zhang^{b, d},
Jun Fang^b,
Genfa Zhang^a,
Chengcai Chu^{a, b, c}

a
Key Laboratory for Cell Proliferation and Regulation Biology of Ministry of Education, College of Life Science, Beijing Normal University, Beijing 100875, China
b
The State Key Laboratory of Plant Genomics and National Plant Gene Research Center (Beijing), Institute of Genetics and Developmental Biology, Chinese Academy of Sciences, Datun Road, Chaoyang District, Beijing 100101, China
c
Graduate School of the Chinese Academy of Sciences, Yuquan Road, Beijing 100039, China
d
Rice Research Institute, Sichuan Agricultural University, Chengdu 611130, China

More Information

Corresponding author: E-mail address: gfzh@bnu.edu.cn (Genfa Zhang); E-mail address: ccchu@genetics.ac.cn (Chengcai Chu)
Received Date: 2010-10-11
Accepted Date: 2010-10-20
Rev Recd Date: 2010-10-17

Available Online: 2011-02-19

Publish Date: 2011-01-20

Abstract

Abstract

Lesion mimic is necrotic lesions on plant leaf or stem in the absence of pathogenic infection, and its exact biological mechanism is varied. By a large-scale screening of our T-DNA mutant population, we identified a mutant rice lesion initiation 1 (rlin1), which was controlled by a single nuclear recessive gene. Map-based cloning revealed that RLIN1 encoded a putative coproporphyrinogen III oxidase in tetrapyrrole biosynthesis pathway. Sequencing results showed that a G to T substitution occurred in the second exon of RLIN1 and led to a missense mutation from Asp to Tyr. Ectopic expression of RLIN1 could rescue rlin1 lesion mimic phenotype. Histochemical analysis demonstrated that lesion formation inrlin1 was light-dependent accompanied by reactive oxygen species accumulated. These results suggest that tetrapyrrole participates in lesion formation in rice.
- Rice,
- Map-based cloning,
- Lesion mimic,
- Coproporphyrinogen III oxidase,
- Tetrapyrrole

These authors contributed equally to this work.

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References(38)

References

[1]	Ayliffe, M.A., Agostino, A., Clarke, B.C. et al. Plant Cell, 21 (2009),pp. 814-831
[2]	Boese, Q.F., Spano, A.J., Li, J.M. et al. J. Biol. Chem., 266 (1991),pp. 17060-17066
[3]	Chou, K.C., Shen, H.B. Cell-PLoc: a package of web servers for predicting subcellular localization of proteins in various organisms Nat. Protoco, 3 (2008),pp. 153-162
[4]	Danon, A., Miersch, O., Felix, G. et al. Plant J., 41 (2005),pp. 68-80
[5]	Edwards, K., Johnstone, C., Thompson, C. A simple and rapid method for the preparation of plant genomic DNA for PCR analysis Nucleic Acids Res., 19 (1991),p. 1349
[6]	Gray, J., Janick-Buckner, D., Buckner, B. et al. Plant Physiol., 130 (2002),pp. 1894-1907
[7]	Grimm, B. Novel insights in the control of tetrapyrrole metabolism of higher plants Curr. Opin. Plant Biol., 1 (1998),pp. 245-250
[8]	Hammond-Kosack, K.E., Jones, J.D.G. Resistance gene-dependent plant defense responses Plant Cell, 8 (1996),pp. 1773-1791
[9]	Hirashima, M., Tanaka, R., Tanaka, A. Plant Cell Physiol., 50 (2009),pp. 719-729
[10]	Hu, G., Yalpani, N., Briggs, S.P. et al. A porphyrin pathway impairment is responsible for the phenotype of a dominant disease lesion mimic mutant of maize Plant Cell, 10 (1998),pp. 1095-1105
[11]	Ishikawa, A. Biosci. Biotechnol. Biochem., 69 (2005),pp. 1929-1934
[12]	Ishikawa, A., Okamoto, H., Iwasaki, Y. et al. Plant J., 27 (2001),pp. 89-99
[13]	Jung, K.H., Hur, J., Ryu, C.H. et al. Characterization of a rice chlorophyll-deficient mutant using the T-DNA gene-trap system Plant Cell Physiol., 44 (2003),pp. 463-472
[14]	Kruse, E., Mock, H.P., Grimm, B. Reduction of coproporphyrinogen oxidase level by antisense RNA synthesis leads to deregulated gene expression of plastid proteins and affects the oxidative defense system EMBO J., 14 (1995),pp. 3712-3720
[15]	Lee, S., Kim, J.H., Yoo, E. et al. Differential regulation of chlorophyll a oxygenase genes in rice Plant Mol. Biol., 57 (2005),pp. 805-818
[16]	Liu, X.Q., Bai, X.Q., Wang, X.J. et al. OsWRKY71, a rice transcription factor, is involved in rice defense response J. Plant Physiol., 164 (2007),pp. 969-979
[17]	Ma, Y.M., Liu, L., Zhu, C.G. et al. Molecular analysis of rice plants harboring a multi-functional T-DNA tagging system J. Genet. Genomics, 36 (2009),pp. 267-276
[18]	Mach, J.M., Castillo, A.R., Hoogstraten, R. et al. Proc. Natl. Acad. Sci. USA, 98 (2001),pp. 771-776
[19]	Matin, M.N., Pandeya, D., Baek, K.H. et al. Phenotypic and genotypic analysis of rice lesion mimic mutants Plant Pathol. J., 26 (2010),pp. 159-169
[20]	Meskauskiene, R., Nater, M., Goslings, D. et al. Proc. Natl. Acad. Sci. USA, 98 (2001),pp. 12826-12831
[21]	Mock, H.P., Grimm, B. Reduction of uroporphyrinogen decarboxylase by antisense RNA expression affects activities of other enzymes involved in tetrapyrrole biosynthesis and leads to light-dependent necrosis Plant Physiol., 113 (1997),pp. 1101-1112
[22]	Mock, H.P., Lermontova, I., Keetman, U. et al. Consequences of photo-oxidation in transgenic tobacco with co-suppression of coproporphyrinogen oxidase Phyton-Ann. Rei. Bot. A, 37 (1997),pp. 169-174
[23]	Mock, H.P., Keetman, U., Kruse, E. et al. Defense responses to tetrapyrrole-induced oxidative stress in transgenic plants with reduced uroporphyrinogen decarboxylase or coproporphyrinogen oxidase activity Plant Physiol., 116 (1998),pp. 107-116
[24]	Mock, H.P., Heller, W., Molina, A. et al. Expression of uroporphyrinogen decarboxylase or coproporphyrinogen oxidase antisense RNA in tobacco induces pathogen defense responses conferring increased resistance to tobacco mosaic virus J. Biol. Chem., 274 (1999),pp. 4231-4238
[25]	Molina, A., Volrath, S., Guyer, D. et al. Plant J., 17 (1999),pp. 667-678
[26]	Nagata, N., Tanaka, R., Satoh, S. et al. Plant Cell, 17 (2005),pp. 233-240
[27]	op den Camp, R.G., Przybyla, D., Ochsenbein, C. et al. Plant Cell, 15 (2003),pp. 2320-2332
[28]	Papenbrock, J., Mishra, S., Mock, H.P. et al. Impaired expression of the plastidic ferrochelatase by antisense RNA synthesis leads to a necrotic phenotype of transformed tobacco plants Plant J., 28 (2001),pp. 41-50
[29]	Tanaka, R., Tanaka, A. Tetrapyrrole biosynthesis in higher plants Annu. Rev. Plant Biol., 58 (2007),pp. 321-346
[30]	Tanaka, R., Hirashima, M., Satoh, S. et al. Plant Cell Physiol., 44 (2003),pp. 1266-1274
[31]	Thordal-Christensen, H., Zhang, Z.G., Wei, Y.D. et al. Plant J., 11 (1997),pp. 1187-1194
[32]	Tong, H., Jin, Y., Liu, W. et al. DWARF AND LOW-TILLERING, a new member of the GRAS family, plays positive roles in brassinosteroid signaling in rice Plant J., 58 (2009),pp. 803-816
[33]	Wagner, D., Przybyla, D., Op den Camp, R. et al. Science, 306 (2004),pp. 1183-1185
[34]	Wang, P., Gao, J., Wan, C. et al. Plant Physiol., 153 (2010),pp. 994-1003
[35]	Wu, Z., Zhang, X., He, B. et al. A chlorophyll-deficient rice mutant with impaired chlorophyllide esterification in chlorophyll biosynthesis Plant Physiol., 145 (2007),pp. 29-40
[36]	Yang, M., Wardzala, E., Johal, G.S. et al. Plant Mol. Biol., 54 (2004),pp. 175-191
[37]	Yang, Z., Wu, Y., Li, Y. et al. OsMT1a, a type 1 metallothionein, plays the pivotal role in zinc homeostasis and drought tolerance in rice Plant Mol. Biol., 70 (2009),pp. 219-229
[38]	Zhang, H.T., Li, J.J., Yoo, J.H. et al. Plant Mol. Biol., 62 (2006),pp. 325-337