Accumulation of Cyanobacterial Photosystem II Containing the ‘Rogue’ D1 Subunit Is Controlled by FtsH Protease and Synthesis of the Standard D1 Protein

Author:

Masuda Takako1,Bečková Martina1,Turóczy Zoltán1,Pilný Jan1,Sobotka Roman12ORCID,Trinugroho Joko P3,Nixon Peter J3,Prášil Ondřej1,Komenda Josef12ORCID

Affiliation:

1. Institute of Microbiology, The Czech Academy of Sciences, Centre Algatech , Opatovický mlýn, Třeboň 37901, Czech Republic

2. Faculty of Science, University of South Bohemia , Branišovská 1760, České Budějovice 370 05, Czech Republic

3. Sir Ernst Chain Building-Wolfson Laboratories, Department of Life Sciences, Imperial College London , South Kensington Campus, London SW7 2AZ, UK

Abstract

Abstract Unicellular diazotrophic cyanobacteria contribute significantly to the photosynthetic productivity of the ocean and the fixation of molecular nitrogen, with photosynthesis occurring during the day and nitrogen fixation during the night. In species like Crocosphaera watsonii WH8501, the decline in photosynthetic activity in the night is accompanied by the disassembly of oxygen-evolving photosystem II (PSII) complexes. Moreover, in the second half of the night phase, a small amount of rogue D1 (rD1), which is related to the standard form of the D1 subunit found in oxygen-evolving PSII, but of unknown function, accumulates but is quickly degraded at the start of the light phase. We show here that the removal of rD1 is independent of the rD1 transcript level, thylakoid redox state and trans-thylakoid pH but requires light and active protein synthesis. We also found that the maximal level of rD1 positively correlates with the maximal level of chlorophyll (Chl) biosynthesis precursors and enzymes, which suggests a possible role for rogue PSII (rPSII) in the activation of Chl biosynthesis just before or upon the onset of light, when new photosystems are synthesized. By studying strains of Synechocystis PCC 6803 expressing Crocosphaera rD1, we found that the accumulation of rD1 is controlled by the light-dependent synthesis of the standard D1 protein, which triggers the fast FtsH2-dependent degradation of rD1. Affinity purification of FLAG-tagged rD1 unequivocally demonstrated the incorporation of rD1 into a non-oxygen-evolving PSII complex, which we term rPSII. The complex lacks the extrinsic proteins stabilizing the oxygen-evolving Mn4CaO5 cluster but contains the Psb27 and Psb28-1 assembly factors.

Funder

Biotechnology and Biological Sciences Research Council

Czech Science Foundation

Publisher

Oxford University Press (OUP)

Subject

Cell Biology,Plant Science,Physiology,General Medicine

同舟云学术

1.学者识别学者识别

2.学术分析学术分析

3.人才评估人才评估

"同舟云学术"是以全球学者为主线,采集、加工和组织学术论文而形成的新型学术文献查询和分析系统,可以对全球学者进行文献检索和人才价值评估。用户可以通过关注某些学科领域的顶尖人物而持续追踪该领域的学科进展和研究前沿。经过近期的数据扩容,当前同舟云学术共收录了国内外主流学术期刊6万余种,收集的期刊论文及会议论文总量共计约1.5亿篇,并以每天添加12000余篇中外论文的速度递增。我们也可以为用户提供个性化、定制化的学者数据。欢迎来电咨询!咨询电话:010-8811{复制后删除}0370

www.globalauthorid.com

TOP

Copyright © 2019-2024 北京同舟云网络信息技术有限公司
京公网安备11010802033243号  京ICP备18003416号-3