A Ca2+-binding motif underlies the unusual properties of certain photosynthetic bacterial core light-harvesting complexes
Tani, Kazutoshi; Kobayashi, Kazumi4; Hosogi, Naoki4; Ji, Xuan-Cheng; Nagashima, Sakiko; Nagashima, Kenji V. P.; Izumida, Airi10; Inoue, Kazuhito2,10; Tsukatani, Yusuke9; Kanno, Ryo
刊名JOURNAL OF BIOLOGICAL CHEMISTRY
2022
卷号298期号:6
DOI10.1016/j.jbc.2022.101967
文献子类Article
英文摘要The mildly thermophilic purple phototrophic bacterium Allochromatium tepidum provides a unique model for investigating various intermediate phenotypes observed between those of thermophilic and mesophilic counterparts. The core light-harvesting (LH1) complex from A. tepidum exhibits an absorption maximum at 890 nm and mildly enhanced thermostability, both of which are Ca2+-dependent. However, it is unknown what structural determinants might contribute to these properties. Here, we present a cryo-EM structure of the reaction center-associated LH1 complex at 2.81 angstrom resolution, in which we identify multiple pigment-binding alpha- and beta-polypeptides within an LH1 ring. Of the 16 alpha-polypeptides, we show that six (alpha 1) bind Ca2+ along with beta 1- or beta 3-polypeptides to form the Ca-2-binding sites. This structure differs from that of fully Ca2+-bound LH1 from Thermochromatium tepidum, enabling determination of the minimum structural requirements for Ca2+-binding. We also identified three amino acids (Trp44, Asp47, and le49) in the C-terminal region of the A. tepidum alpha 1-polypeptide that ligate each Ca ion, forming a Ca2+-binding WxxDxl motif that is conserved in all Ca2+ bound LH1 alpha-polypeptides from other species with reported structures. The partial Ca-2-bound structure further explains the unusual phenotypic properties observed for this bacterium in terms of its Ca2+-requirements for thermostability, spectroscopy, and phototrophic growth, and supports the hypothesis that A. tepidum may represent a transitional species between mesophilic and thermophilic purple sulfur bacteria. The characteristic arrangement of multiple appolypeptides also suggests a mechanism of molecular recognition in the expression and/or assembly of the LH1 complex that could be regulated through interactions with reaction center subunits.
学科主题Biochemistry & Molecular Biology
电子版国际标准刊号1083-351X
出版地AMSTERDAM
WOS关键词Q(Y) RED-SHIFT ; LH1-RC COMPLEX ; THERMOCHROMATIUM-TEPIDUM ; CALCIUM-IONS ; BACTERIOCHLOROPHYLL ; SYSTEM ; THERMOSTABILITY
WOS研究方向Science Citation Index Expanded (SCI-EXPANDED)
语种英语
出版者ELSEVIER
WOS记录号WOS:000994013900001
资助机构National Key R&D Program of China [2019YFA0904600]
内容类型期刊论文
源URL[http://ir.ibcas.ac.cn/handle/2S10CLM1/28967]  
专题中科院光生物学重点实验室
作者单位1.Kanno, Ryo; Hall, Malgorzata; Humbel, Bruno M.] Okinawa Inst Sci & Technol Grad Univ OIST, Res Support Div, Imaging Sect, Okinawa, Japan
2.Ibaraki Univ, Fac Sci, Mito, Ibaraki, Japan
3.JEOL Ltd, EM Business Unit, 3-1-2 Musashino, Akishima, Tokyo, Japan
4.Mie Univ, Grad Sch Med, Tsu, Mie, Japan
5.Kobe Univ, Grad Sch Agr, Dept Agrobiosci, Kobe, Hyogo, Japan
6.Madigan, Michael T.] Southern Illinois Univ, Sch Biol Sci, Dept Microbiol, Carbondale, IL USA
7.Chinese Acad Sci, Inst Bot, Photosynthesis Res Ctr, Key Lab Photobiol, Beijing, Peoples R China
8.Japan Agcy Marine Earth Sci & Technol JAMSTEC, Inst Extra Cutting Edge Sci & Technol Avant Garde, Yokosuka, Kanagawa, Japan
9.Kanagawa Univ, Dept Biol Sci, Fac Sci, Hiratsuka, Kanagawa, Japan
10.Kanagawa Univ, Res Inst Integrated Sci, Fac Sci, Hiratsuka, Kanagawa, Japan
推荐引用方式
GB/T 7714
Tani, Kazutoshi,Kobayashi, Kazumi,Hosogi, Naoki,et al. A Ca2+-binding motif underlies the unusual properties of certain photosynthetic bacterial core light-harvesting complexes[J]. JOURNAL OF BIOLOGICAL CHEMISTRY,2022,298(6).
APA Tani, Kazutoshi.,Kobayashi, Kazumi.,Hosogi, Naoki.,Ji, Xuan-Cheng.,Nagashima, Sakiko.,...&Wang-Otomo, Zheng-Yu.(2022).A Ca2+-binding motif underlies the unusual properties of certain photosynthetic bacterial core light-harvesting complexes.JOURNAL OF BIOLOGICAL CHEMISTRY,298(6).
MLA Tani, Kazutoshi,et al."A Ca2+-binding motif underlies the unusual properties of certain photosynthetic bacterial core light-harvesting complexes".JOURNAL OF BIOLOGICAL CHEMISTRY 298.6(2022).
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