CpeT is the phycoerythrobilin lyase for Cys-165 on β-phycoerythrin from Fremyella diplosiphon and the chaperone-like protein CpeZ greatly improves its activity

Nguyen, Adam A.; Joseph, Kes Lynn; Bussell, Adam N.; Pokhrel, Suman; Karty, Jonathan A.; Kronfel, Christina M.; Kehoe, David M.; Schluchter, Wendy M.

doi:10.1016/j.bbabio.2020.148284

Cited by 7 publications

(6 citation statements)

References 43 publications

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“…Homologs of cpeZ in the two thermophiles may function as chaperones, facilitating cpeF and cpeB interaction by stabilizing cpeB s conformation [ 44 ]. Moreover, homologs of cpeS , cpeT , and cpeU in the two thermophiles may attach PEB to Cys residues of the cpeB subunit of PE [ 44 , 45 ].…”

Section: Resultsmentioning

confidence: 99%

“…Although PE-associated genes are widely distributed in a large region, they may directly or indirectly regulate each other. For instance, the cpeT mutant strain of Tolypothrix PCC 7601 showed the downregulation of cpeB-A and the upregulation of the cpeCDESTR operon, suggesting potential regulatory roles of cpeT on the expression of these genes in addition to its role as a PEB lyase for chromophorylation on the β-subunit of PE [ 45 ]. The chromophorylation efficiency of CpeT can be improved with the help of the chaperone-like protein CpeZ, which can also facilitate the lyase activity of CpeS, CpeT, and CpeU [ 43 , 50 ].…”

Section: Resultsmentioning

confidence: 99%

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Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria

Tang

Zhou

Yao

et al. 2023

IJMS

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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 Leptolyngbya, Leptothermofonsia, Ocullathermofonsia, Thermoleptolyngbya, Trichothermofonsia, Synechococcus, Thermostichus, and Thermosynechococcus. 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 apcE indicate a photoacclimation of a far-red light by Leptolyngbya JSC-1, Leptothermofonsia E412, and Ocullathermofonsia A174. The composition pattern of phycobilin lyases is consistent among the thermophiles, except for Thermostichus strains that have extra homologs of cpcE, cpcF, and cpcT. 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.

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Section: Resultsmentioning

confidence: 99%

Section: Resultsmentioning

confidence: 99%

Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria

Tang

Zhou

Yao

et al. 2023

IJMS

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“…It has been reported that these enzymes are responsible for the binding of PCB and PEB at cysteine residue 153 of the β subunit of phycocyanin and phycoerythrocyanin [52] . Recent studies on the CpeT lyase suggest that this enzyme could be responsible for the binding of PEB at residues 155 of PE [64] . Table 2 shows a summary of lyase enzymes and their activity on PBPs.…”

Section: Phycobiliprotein Maturationmentioning

confidence: 99%

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Dagnino‐Leone

Figueroa

Castañeda

et al. 2022

Computational and Structural Biotechnology Journal

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“…Both S-CAM7-like viral genomes contain auxiliary metabolic genes (AMGs) previously described in cyanophage (Table S7). Notably, each virus contained the photosynthesis-related AMGs for cp12 , a gene responsible for inhibiting the Calvin Cycle during infections in the light 54 , and cpeT , a bilin lyase, important for pigment adaptation in the freshwater cyanobacteria Fremyella diplosiphon 55 . These two genes are commonly reported in cyanophage genomes but are not present in the S-CAM7 0910SB42 genome 53 .…”

Section: Resultsmentioning

confidence: 99%

Hi-C assembled genomes of estuarine populations reveal virus-microbe associations and a broad interaction range of a cyanophage

Rathwell,

McKay,

Rocap

2023

Preprint

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Aquatic microbes play key roles in global biogeochemical cycles and their viral-induced mortality influences the flow of carbon and nutrients between the dissolved and particulate pools. However, many microbes remain uncultivated, hindering understanding of their metabolic capabilities and preventing isolation of viruses that infect them. Here we augment metagenomic sequencing with Hi-C, a proximity-linkage method whereby DNA within a cell is physically bound and then sequenced to link contigs within a metagenome that originated from the same cell. In a size-fractioned water sample from beneath the euphotic zone in a hypoxic estuarine fjord in Puget Sound, WA we resolved 49 proximity-linked bins above 50% complete, including 21 Hi-C Assembled Genomes (HAGs) over 90% complete and a nearly complete genome of the eukaryotic green algaPicochlorum. Viral and microbial sequence within the same HAG identified 18 virus-microbe interactions. A myovirus and a siphovirus were associated with 2 different genera within the Saltatorellus clade of Planctomycetes, a phylum for which no virus has been identified. A partialPhycodnaviridaegenome linked to Haptophyte sequence is consistent with contemporaneous observations of a dissipating coccolithophore bloom. A cyanophage S-CAM7-like sequence had a broad interaction range. It was associated with a partialSynechococcusgenome in the >3.0 µm size fraction and with a Gammaproteobacteria related toAlcanivoraxin the 0.2µm-3.0µm fraction. We suggest that viruses produced in surface waters that are shuttled to depth on sinking aggregates may interact with different hosts in deeper waters, providing an important avenue for gene transfer across broad taxonomic ranges.ImportanceAquatic microbes are important in global elemental cycling. Knowing which viruses infect them in the environment remains a challenge. Using Hi-C, a molecular technique to physically link DNA within a cell, we assembled nearly complete genomes of both prokaryotes and eukaryotes from a hypoxic estuary. Hi-C links captured virus-host interactions for known virus-host pairs and for hosts with no previously known viruses. The same virus was linked to two distinct microbes in different size fractions of water, suggesting it has a broad host range. Viral lysis in surface waters generates sinking particles that deliver newly produced viruses to deeper waters where they interact with different potential hosts, providing an opportunity for gene exchange between unrelated microbes.

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CpeT is the phycoerythrobilin lyase for Cys-165 on β-phycoerythrin from Fremyella diplosiphon and the chaperone-like protein CpeZ greatly improves its activity

Cited by 7 publications

References 43 publications

Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria

Characterization of Molecular Diversity and Organization of Phycobilisomes in Thermophilic Cyanobacteria

Phycobiliproteins: Structural aspects, functional characteristics, and biotechnological perspectives

Hi-C assembled genomes of estuarine populations reveal virus-microbe associations and a broad interaction range of a cyanophage

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