Structure of the novel 14kDa fragment of α-subunit of phycoerythrin from the starving cyanobacterium Phormidium tenue

Soni, Badrish; Hasan, Md. Imtaiyaz; Parmar, Asha; Ethayathulla, A.S.; Kumar, Rajeev; Singh, Niraj Kumar; Sinha, Mau; Kaur, Punit; Yadav, Savita; Sharma, Sujata; Madamwar, Datta

doi:10.1016/j.jsb.2010.05.008

Cited by 20 publications

(24 citation statements)

References 46 publications

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“…It is well known that some Phormidium species contain phycoerythrin (Marquardt and Palinska, 2007; Marquardt, 2008;Palinska et al, 2011;Soni et al, 2010). The patterns of absorbance and fluorescence of natural biofilms dominated by cyanobacteria and cultures observed in this study demonstrate that green and brown samples can be distinguished by the presence/absence of PE.…”

Section: Discussionsupporting

confidence: 49%

Application of a spectrofluorimetric tool (bbe BenthoTorch) for monitoring potentially toxic benthic cyanobacteria in rivers

Echenique‐Subiabre¹,

Dalle²,

Duval³

et al. 2016

Water Research

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Section: Discussionsupporting

confidence: 49%

Application of a spectrofluorimetric tool (bbe BenthoTorch) for monitoring potentially toxic benthic cyanobacteria in rivers

Echenique‐Subiabre¹,

Dalle²,

Duval³

et al. 2016

Water Research

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“…PE is made up of two peptides, namely, α-and β-subunits containing amino acids ranging from 160 to 180 (Anwer et al 2015;Soni et al 2010). Both the subunits contain covalently attached open chain tetra-pyrrole chromophore/s-the phycoerythrobilin (PEB) (Apt et al 1995).…”

mentioning

confidence: 99%

Phycoerythrin averts intracellular ROS generation and physiological functional decline in eukaryotes under oxidative stress

Sonani

Rastogi

Singh³

et al. 2016

Protoplasma

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In vitro antioxidant virtue and life-prolonging effect of phycoerythrin (PE; a pigment protein isolated from Phormidium sp. A09DM) have been revealed in our previous reports (Sonani et al. in Age 36:9717, 2014a; Sonani et al. in Process Biochem 49:1757-1766, 2014b). It has been hypothesized that the PE expands life span of Caenorhabditis elegans (bears large resemblance with human aging pathways) due to its antioxidant virtue. This hypothesis is tested in present study by checking the effect of PE on intracellular reactive oxygen species (ROS) generation and associated physiological deformities using mouse and human skin fibroblasts, C. elegans, and Drosophila melanogaster Oregon R and by divulging PE's structural attributes responsible for its antioxidant asset. PE treatment displayed noteworthy decrease of 67, 48, and 77 % in ROS level in mouse fibroblast (3T3-L1), human fibroblast, and C. elegans N2, respectively, arisen under chemical-induced oxidative stress. PE treatment delayed the development of paraquat-induced Alzheimer phenotype by 14.5 % in C. elegans CL4176. Furthermore, PE improved the locomotion of D. melanogaster Oregon R under oxidative stress with simultaneous up-regulation in super-oxide dismutase and catalase activities. The existence of 52 Glu + Asp + His + Thr residues (having metal ion sequestration capacity), 5 phycoerythrobilin chromophores (potential electron exchangers) in PE's primary structure, and significant hydrophobic patches on the surface of its α- and β-subunits are supposed to collectively contribute in the antioxidant virtues of PE. Altogether, results support the hypothesis that it is the PE's antioxidant asset, which is responsible for its life-prolonging effect and thus could be exploited in the therapeutics of ROS-associated abnormalities including aging and neurodegeneration in eukaryotes.

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“…C-PE contains 6α and 6β subunits arranged in ring-like assemblies where the three monomers are present in the three-fold symmetry (Chang et al, 1996;Soni et al, 2010). Each α-subunit of PE consists of 164 residues, while each β-subunit contains 171 residues (MacColl, 1998;Soni et al, 2010). The structure of C-PE resembles with globin proteins which contain two open-chain linear tetrapyrolle chromophores called phycoerythrobilins (PEBs), which are covalently attached with each α-subunit at Cys82 and Cys139.…”

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confidence: 99%

“…The structure of C-PE resembles with globin proteins which contain two open-chain linear tetrapyrolle chromophores called phycoerythrobilins (PEBs), which are covalently attached with each α-subunit at Cys82 and Cys139. While β-subunit of C-PE contains three PEBs of which two are covalently attached with Cys84 and Cys155, the third chromophore is doubly linked to Cys50 and Cys6 (Chang et al, 1996;MacColl, 1998;Soni et al, 2010). The interactions between PEB with protein atoms as well as protein-chromophore environments are critically responsible for the photon absorption properties of C-PE.…”

mentioning

confidence: 99%

“…Recently, we have identified and determined the crystal structure of α-subunit of C-PE (αC-PE) from Phormidium tenue, which is devoid of 31 residues from its amino terminal side (Soni et al, 2010), as compared to all other α-PEs including that of red algae (α-RPE) Polysiphonia urceolata containing complete 164 residues (Chang et al, 1996). It is interesting to note that truncation of 31 residues occur naturally when the organism is grown or kept in prolonged starved condition.…”

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confidence: 99%

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Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies

Anwer

Sonani

Madamwar

et al. 2013

Journal of Biomolecular Structure and Dynamics

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The conformational state of biliproteins can be determined by optical properties of the covalently linked chromophores. Recently determined crystal structure of truncated form of α-subunit of cyanobacterial phycoerythrin (αC-PE) from Phormidium tenue provides a new insight into the structure-function relationship of αC-PE. To compare their stabilities, we have measured urea-induced denaturation transitions of the full length αC-PE (FL-αC-PE) and truncated αC-PE (Tr-αC-PE) followed by observing changes in absorbance at 565 nm, fluorescence at 350 and 573 nm, and circular dichroism at 222 nm as a function of [urea], the molar concentration of urea. The transition curve of each protein was analyzed for ΔG(D)(0), the value of Gibbs free energy change on denaturation (ΔG(D)) in the absence of urea; m, the slope (=∂∆G(D)/∂[urea]), and C(m), the midpoint of the denaturation curve, i.e. [urea] at which ΔG(D) = 0. A difference of about 10% in ΔG(D)(0) observed between FL-αC-PE and Tr-αC-PE, suggests that the two proteins are almost equally stable, and the natural deletion of 31 residues from the N-terminal side of the full length protein does not alter its stability. Furthermore, normalization of probes shows that the urea-induced denaturation of both the proteins is a two-state process. Folding of both structural variants (Tr-αC-PE and FL-αC-PE) of P. tenue were also studied using molecular dynamics simulations at 300 K. The results show clearly that the stability of the proteins is evenly distributed over the whole structure indicating no significant role of N-terminal residues in the stability of both proteins.

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Structure of the novel 14kDa fragment of α-subunit of phycoerythrin from the starving cyanobacterium Phormidium tenue

Cited by 20 publications

References 46 publications

Application of a spectrofluorimetric tool (bbe BenthoTorch) for monitoring potentially toxic benthic cyanobacteria in rivers

Application of a spectrofluorimetric tool (bbe BenthoTorch) for monitoring potentially toxic benthic cyanobacteria in rivers

Phycoerythrin averts intracellular ROS generation and physiological functional decline in eukaryotes under oxidative stress

Role of N-terminal residues on folding and stability of C-phycoerythrin: simulation and urea-induced denaturation studies

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