Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria
Thermophilic cyanobacteria are cosmopolitan and abundant in the thermal environment. Their light-harvesting complexes, phycobilisomes (PBS), are highly important in photosynthesis. To date, there is limited information on the PBS composition of thermophilic cyanobacteria whose habitats are challengi...
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MDPI AG
2023-03-01
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| Series: | International Journal of Molecular Sciences |
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| author | Jie Tang Huizhen Zhou Dan Yao Lianming Du Maurycy Daroch |
| author_facet | Jie Tang Huizhen Zhou Dan Yao Lianming Du Maurycy Daroch |
| author_sort | Jie Tang |
| collection | DOAJ |
| description | Thermophilic cyanobacteria are cosmopolitan and abundant in the thermal environment. Their light-harvesting complexes, phycobilisomes (PBS), are highly important in photosynthesis. To date, there is limited information on the PBS composition of thermophilic cyanobacteria whose habitats are challenging for survival. Herein, genome-based methods were used to investigate the molecular components of PBS in 19 well-described thermophilic cyanobacteria. These cyanobacteria are from the genera <i>Leptolyngbya</i>, <i>Leptothermofonsia</i>, <i>Ocullathermofonsia</i>, <i>Thermoleptolyngbya</i>, <i>Trichothermofonsia</i>, <i>Synechococcus</i>, <i>Thermostichus</i>, and <i>Thermosynechococcus</i>. According to the phycobiliprotein (PBP) composition of the rods, two pigment types are observed in these thermophiles. The amino acid sequence analysis of different PBP subunits suggests several highly conserved cysteine residues in these thermophiles. Certain amino acid contents in the PBP of thermophiles are significantly higher than their mesophilic counterparts, highlighting the potential roles of specific substitutions of amino acid in the adaptive thermostability of light-harvesting complexes in thermophilic cyanobacteria. Genes encoding PBS linker polypeptides vary among the thermophiles. Intriguingly, motifs in linker <i>apcE</i> indicate a photoacclimation of a far-red light by <i>Leptolyngbya</i> JSC-1, <i>Leptothermofonsia</i> E412, and <i>Ocullathermofonsia</i> A174. The composition pattern of phycobilin lyases is consistent among the thermophiles, except for <i>Thermostichus</i> strains that have extra homologs of <i>cpcE</i>, <i>cpcF</i>, and <i>cpcT</i>. In addition, phylogenetic analyses of genes coding for PBPs, linkers, and lyases suggest extensive genetic diversity among these thermophiles, which is further discussed with the domain analyses. Moreover, comparative genomic analysis suggests different genomic distributions of PBS-related genes among the thermophiles, indicating probably various regulations of expression. In summary, the comparative analysis elucidates distinct molecular components and organization of PBS in thermophilic cyanobacteria. These results provide insights into the PBS components of thermophilic cyanobacteria and fundamental knowledge for future research regarding structures, functions, and photosynthetic improvement. |
| first_indexed | 2024-03-11T06:25:12Z |
| format | Article |
| id | doaj.art-97875becabd146738a48a70929b01de2 |
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| issn | 1661-6596 1422-0067 |
| language | English |
| last_indexed | 2024-03-11T06:25:12Z |
| publishDate | 2023-03-01 |
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| spelling | doaj.art-97875becabd146738a48a70929b01de22023-11-17T11:36:47ZengMDPI AGInternational Journal of Molecular Sciences1661-65961422-00672023-03-01246563210.3390/ijms24065632Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic CyanobacteriaJie Tang0Huizhen Zhou1Dan Yao2Lianming Du3Maurycy Daroch4School of Food and Bioengineering, Chengdu University, Chengdu 610106, ChinaSchool of Food and Bioengineering, Chengdu University, Chengdu 610106, ChinaSchool of Food and Bioengineering, Chengdu University, Chengdu 610106, ChinaSchool of Food and Bioengineering, Chengdu University, Chengdu 610106, ChinaSchool of Environment and Energy, Peking University Shenzhen Graduate School, 2199 Lishui Road, Shenzhen 518055, ChinaThermophilic cyanobacteria are cosmopolitan and abundant in the thermal environment. Their light-harvesting complexes, phycobilisomes (PBS), are highly important in photosynthesis. To date, there is limited information on the PBS composition of thermophilic cyanobacteria whose habitats are challenging for survival. Herein, genome-based methods were used to investigate the molecular components of PBS in 19 well-described thermophilic cyanobacteria. These cyanobacteria are from the genera <i>Leptolyngbya</i>, <i>Leptothermofonsia</i>, <i>Ocullathermofonsia</i>, <i>Thermoleptolyngbya</i>, <i>Trichothermofonsia</i>, <i>Synechococcus</i>, <i>Thermostichus</i>, and <i>Thermosynechococcus</i>. According to the phycobiliprotein (PBP) composition of the rods, two pigment types are observed in these thermophiles. The amino acid sequence analysis of different PBP subunits suggests several highly conserved cysteine residues in these thermophiles. Certain amino acid contents in the PBP of thermophiles are significantly higher than their mesophilic counterparts, highlighting the potential roles of specific substitutions of amino acid in the adaptive thermostability of light-harvesting complexes in thermophilic cyanobacteria. Genes encoding PBS linker polypeptides vary among the thermophiles. Intriguingly, motifs in linker <i>apcE</i> indicate a photoacclimation of a far-red light by <i>Leptolyngbya</i> JSC-1, <i>Leptothermofonsia</i> E412, and <i>Ocullathermofonsia</i> A174. The composition pattern of phycobilin lyases is consistent among the thermophiles, except for <i>Thermostichus</i> strains that have extra homologs of <i>cpcE</i>, <i>cpcF</i>, and <i>cpcT</i>. In addition, phylogenetic analyses of genes coding for PBPs, linkers, and lyases suggest extensive genetic diversity among these thermophiles, which is further discussed with the domain analyses. Moreover, comparative genomic analysis suggests different genomic distributions of PBS-related genes among the thermophiles, indicating probably various regulations of expression. In summary, the comparative analysis elucidates distinct molecular components and organization of PBS in thermophilic cyanobacteria. These results provide insights into the PBS components of thermophilic cyanobacteria and fundamental knowledge for future research regarding structures, functions, and photosynthetic improvement.https://www.mdpi.com/1422-0067/24/6/5632thermophilic cyanobacteriumphycobiliproteinphycobilisomelinker proteinlyase |
| spellingShingle | Jie Tang Huizhen Zhou Dan Yao Lianming Du Maurycy Daroch Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria International Journal of Molecular Sciences thermophilic cyanobacterium phycobiliprotein phycobilisome linker protein lyase |
| title | Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria |
| title_full | Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria |
| title_fullStr | Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria |
| title_full_unstemmed | Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria |
| title_short | Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria |
| title_sort | characterization of molecular diversity and organization of phycobilisomes in thermophilic cyanobacteria |
| topic | thermophilic cyanobacterium phycobiliprotein phycobilisome linker protein lyase |
| url | https://www.mdpi.com/1422-0067/24/6/5632 |
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