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PALE-GREEN LEAF 1, a rice cpSRP54 protein, is essential for the assembly of the PSI-LHCI supercomplex

文献类型： 外文期刊

作者： Gao, Peng 1 ; Xia, Haoqiang 2 ; Li, Qiang 3 ; Li, Zongzhu 2 ; Zhai, Chun 1 ; Weng, Lin 2 ; Mi, Hualing 2 ; Yan, Song 4 ; Datla, Raju 5 ; Wang, Hua 6 ; Yang, Jun 2 ;

作者机构： 1.Agr & Agri Food Canada, Saskatoon Res & Dev Ctr, Saskatoon, SK, Canada

2.Chinese Acad Sci, CAS Ctr Excellence Mol Plant Sci, Inst Plant Physiol & Ecol, Natl Key Lab Plant Mol Genet, Shanghai 200032, Peoples R China

3.Huazhong Agr Univ, Natl Key Lab Crop Genet Improvement, Wuhan, Peoples R China

4.Jiangxi Acad Agr Sci, Rice Res Inst, Nanchang, Jiangxi, Peoples R China

5.Univ Saskatchewan, Global Inst Food Secur, Saskatoon, SK S7N 4L8, Canada

6.Zhejiang Acad Agr Sci, Inst Virol & Biotechnol, State Key Lab Managing Biot & Chem Threats Qual &, Hangzhou 310021, Peoples R China

关键词： chloroplast; cpSRP54; PALE-GREEN LEAF 1; photosystem I complex assembly; rice

期刊名称：PLANT DIRECT （ 影响因子：3.369； 五年影响因子：3.457 ）

ISSN：

年卷期： 2022 年 6 卷 8 期

页码：

收录情况： SCI

摘要： Although photosynthetic multiprotein complexes have received major attention, our knowledge about the assembly of these proteins into functional complexes in plants is still limited. In the present study, we have identified a chlorophyll-deficient mutant, pale-green leaf 1 (pgl1), in rice that displays abnormally developed chloroplasts. Map-based cloning of this gene revealed that OsPGL1 encodes a chloroplast targeted protein homologous to the 54-kDa subunit of the signal recognition particle (cpSRP54). Immunoblot analysis revealed that the accumulation of the PSI core proteins PsaA and PsaB, subunits from the ATP synthase, cytochrome, and light-harvesting complex (LHC) is dramatically reduced in pgl1. Blue native gel analysis of thylakoid membrane proteins showed the existence of an extra band in the pgl1 mutant, which located between the dimeric PSII/PSI-LHCI and the monomeric PSII. Immunodetection after 2D separation indicated that the extra band consists of the proteins from the PSI core complex. Measurements of chlorophyll fluorescence at 77 K further confirmed that PSI, rather than PSII, was primarily impaired in the pgl1 mutant. These results suggest that OsPGL1 might act as a molecular chaperone that is required for the efficient assembly and specific integration of the peripheral LHCI proteins into the PSI core complex in rice.

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