Localization of OsTLP27 in thylakoid lumen is required for accumulation of photosynthetic proteins in rice
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We previously identified an AtTLP homolog, OsTLP27, in rice, whose overexpression improves chloroplast ultrastructure and photochemical efficiency. However, its molecular role in photosystem (PS) function and the related signaling pathway remain to be elucidated. In this study, using RNAi strategy, OsTLP27-RNAi transgenic plants displayed normal phenotype in medium containing sucrose, but showed growth retardation when transferred to soil under natural growth conditions. Gene expression showed that chloroplast-related genes were affected, and Western blot analysis revealed that accumulation of photosynthetic proteins was reduced significantly, indicating that OsTLP27 was important to normal PS function. Chloroplast subfraction and trypsin protection analysis showed that OsTLP27 localized in the thylakoid lumen. A yeast two-hybrid experiment revealed that OsTLP27 interacts with ribosomal protein L31 and an aldo–keto reductase (AKR) family protein. Our results suggested that OsTLP27 functions in photosynthetic protein accumulation by interacting with L31 and AKR.
KeywordsRice Thylakoid lumen Chloroplast OsTLP27 Photosystem (PS)
This work was supported by the National Genetically Modified Organisms Breeding Major Projects (2009ZX08009-109B), the National Natural Science Foundation of China (31271685) and the National Key Technology R&D Program of China (2011BAD35B02-05) as well as the Public Experiment Center of State Bioindustrial Base (Chongqing).
- Friso G, Giacomelli L, Ytterberg AJ, Peltier JB, Rudella A, Sun Q, Wijk KJ (2004) In-depth analysis of the thylakoid membrane proteome of Arabidopsis thaliana chloroplasts: new proteins, new functions, and a plastid proteome database. Plant Cell 16(2):478–499PubMedCentralPubMedCrossRefGoogle Scholar
- Jin H, Liu B, Luo L, Feng D, Wang P, Liu J, Da Q, He Y, Qi K, Wang J, Wang HB (2014) HYPERSENSITIVE TO HIGH LIGHT1 interacts with LOW QUANTUM YIELD OF PHOTOSYSTEM II1 and functions in protection of photosystem II from photodamage in Arabidopsis. Plant Cell 26(3):1213–1229PubMedCentralPubMedCrossRefGoogle Scholar
- Kohoutova J, Kuta Smatanova I, Brynda J, Lapkouski M, Revuelta JL, Arellano JB, Ettrich R (2009) Crystallization and preliminary crystallographic characterization of the extrinsic PsbP protein of photosystem II from Spinacia oleracea. Acta Crystallogr Sect F Struct Biol Cryst Commun 65(Pt 2):111–115PubMedCentralPubMedCrossRefGoogle Scholar
- Komenda J, Nickelsen J, Tichy M, Prasil O, Eichacker LA, Nixon PJ (2008) The cyanobacterial homologue of HCF136/YCF48 is a component of an early photosystem II assembly complex and is important for both the efficient assembly and repair of photosystem II in Synechocystis sp. PCC 6803. J Biol Chem 283(33):22390–22399PubMedCrossRefGoogle Scholar
- Zou HY, Wenwen YH, Zang GC, Kang ZH, Zhang ZY, Huang JL, Wang GX (2015) OsEXPB2, a β-expansin gene, is involved in rice root system architecture. Mol Breed 35(1). doi: 10.1007/s11032-015-0203-y