Proposed physiological mode of action of rice hemopexin fold protein OsHFP: linking heme-binding with plant cell death

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• 作者：Tirthartha Chattopadhyay ; Prabir Kumar Das ; Sheuli Roy…
• 关键词：5 ; Aminolevulinic acid ; Heme ; OsHFP ; Oxidative stress ; Cell death ; Tetrapyrrole biosynthesis
• 刊名：Acta Physiologiae Plantarum
• 出版年：2015
• 出版时间：May 2015
• 年：2015
• 卷：37
• 期：5
• 全文大小：3,254 KB
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• 作者单位：Tirthartha Chattopadhyay (1) (2)
  Prabir Kumar Das (3)
  Sheuli Roy (1)
  Mrinal K. Maiti (1) (3)
  
  1. Department of Biotechnology and Advanced Laboratory for Plant Genetic Engineering, Advanced Technology Development Center, Indian Institute of Technology Kharagpur, Kharagpur, 721302, India
  2. Department of Plant Breeding and Genetics, Bihar Agricultural University, Sabour, Bhagalpur, 813210, Bihar, India
  3. Department of Biotechnology, Indian Institute of Technology Kharagpur, Kharagpur, 721302, India
  
• 刊物主题：Plant Physiology; Plant Genetics & Genomics; Plant Biochemistry; Plant Pathology; Plant Anatomy/Development; Agriculture;
• 出版者：Springer Berlin Heidelberg
• ISSN：1861-1664

文摘

The biosynthetic pathway of tetrapyrrole is under stringent regulation in living systems. Heme, one of the products of this branched pathway is well known to regulate the pathway through feedback inhibition. Since the accumulation of intermediates of tetrapyrrole biosynthetic pathway is found to be cytotoxic and inducer of plant programmed cell death through retrograde signalling, certain role of heme in regulating plant cell death is quite logical. In the present study, we report the in vivo heme-binding property of OsHFP, a novel hemopexin fold protein from the rice (Oryza sativa) plant, and document the effect of heme–OsHFP interaction on oxidative stress responses in bacterial and plant systems. The bound heme is retained by the OsHFP even in presence of SDS, and the amount of bound heme to OsHFP increases upon exogenous application of heme biosynthetic precursor in Escherichia coli. In heme-replete condition, the recombinant OsHFP alters the oxidative stress response in E. coli. Ectopic expression of the OsHFP generates oxidative stress in tobacco leaves, which is visualized through the induction of superoxide dismutase activity and localized accumulation of H₂O₂. On the basis of the findings from the present study and the available literature, we propose a possible mode of action of OsHFP in regulating cell death in plant system, which might signify the yet-to-be-deciphered physiological role of hemopexin fold proteins in plants.