Wheat truncated hemoglobin interacts with photosystem I PSK-I subunit and photosystem II subunit PsbS1
- 473 Downloads
Recently, the truncated hemoglobin gene (trHb) was discovered in plant species, however, its role has not yet been determined. In this study, the gene expression of wheat trHb (TatrHb) was analyzed under various biotic and abiotic stresses. TatrHb transcript levels increased in NaCl-treated leaves and gibberellic acid (GA3)-treated roots. In addition, sodium nitroprusside (SNP), a nitric oxide donor, induced an increase in TatrHb transcript levels in roots and leaves. A yeast two-hybrid assay (YIIH) was used to screen a hypoxia-treated wheat seedling library with the goal of determining the putative function of TatrHb. In this YIIH assay, photosynthesis-related genes that showed high homology to the Hordeum vulgare chloroplast photosystem I PSK-I subunit and Zea mays photosystem II subunit PsbS1 were detected and their interactions with TatrHb were confirmed. Subcellular localization of a TatrHb-green fluorescent protein (GFP) fusion protein and bimolecular fluorescence complementation (BiFC) assay suggested that TatrHb is involved in photosynthesis. The TatrHb-GFP fusion protein was localized in the plastids and the yellow fluorescent protein signal indicated that the TatrHb protein interacted with PSK-I and PsbS1 in the chloroplast.
Additional key wordschloroplast gibberellic acid NaCl Triticum aestivum nitric oxide photosynthesis YIIH assay
bimolecular fluorescence complementation
green fluorescent protein
reverse transcriptase-polymerase chain reaction
Triticum aestivum L. truncated hemoglobin
yellow fluorescent protein
Unable to display preview. Download preview PDF.
- Appleby, C.A.: The origin and functions of hemoglobin in plants. — Sci. Progr. 76: 365–398, 1992.Google Scholar
- Chen, H., Nelson, R.S., Sherwood, J.L.: Enhanced recovery of transformants of Agrobacterium tumefaciens after freezethaw transformation and drug selection. — Biotechnology 16: 664–670, 1994.Google Scholar
- Sakamoto, A., Sakurao, S.H., Fukunaga, K., Matsubara, T., Ueda-Hashimoto, M., Tsukamoto, S., Takahashi, M., Morikawa, H.: Three distinct Arabidopsis hemoglobins exhibit peroxidase-like activity and differentially mediate nitritedependent protein nitration. — FEBS Lett. 572: 27–32, 2004.PubMedCrossRefGoogle Scholar
- Trent, J.T., Hargrove, M.S.: A ubiquitously expressed human hexacoordinate hemoglobin. — J. Biochem. 277: 19538–19545, 2002.Google Scholar
- Walter, M., Chaban, C., Schütze, K., Batistic, O., Weckermann, K., Näke, C., Blazevic, D., Grefen, C., Schumacher, K., Oecking, C., Harter, K., Kudla, J.: Visualization of protein interactions in living plant cells using bimolecular fluorescence complementation. — Plant J. 40: 428–438, 2004.PubMedCrossRefGoogle Scholar
- Zhang, B., Wang, H. Q., Liu, B. L., Liu, J., Wang, X., Liu Q., Zhang H. G.: A potato NOA gene increased salinity tolerance in Arabidopsis thaliana. — Afr. J. Biotechnol. 9: 5869–5878, 2010.Google Scholar