The phycobilisomes of the cyanobacterium Arthrospira (Spirulina) maxima

Gómez-Lojero, Carlos; Pérez-Gómez, Bertha; Prado-Flores, Guadalupe; Krogmann, David W.; Cárabez-Trejo, Alfonso; Peña-Díaz, Antonio

doi:10.1016/s1357-2725(97)00043-5

Cited by 12 publications

(3 citation statements)

References 48 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Manual crushing of biomass with or without using an abrasive is also reported in some studies (Gómez-Lojero et al, 1997;Munier et al, 2014). Due to generation of heat from the crushing process, the CPE extracted runs the risk of being denatured even before it is completely extracted into the buffer.…”

Section: Choice Of Buffer and Cell Disruption Methods Influence Cpe Extractionmentioning

confidence: 99%

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Ghosh

Mishra

2020

Front. Sustain. Food Syst.

View full text Add to dashboard Cite

Being a naturally produced colorant with fluorescent properties, C-phycoerythrin (CPE) has important food industry applications. However, optimization of extraction and its stability under storage is an aspect which needs further attention. In this study, optimization of CPE extraction from Lyngbya sp. CCNM 2053 was undertaken using response surface methodology (RSM). Preliminary screening suggested a phosphate buffered system with freeze thaw for cell disruption as the most suitable method. 22.40 ± 1.31 mg g −1 CPE and 52.76 ± 0.07 mg g −1 total proteins were extracted using phosphate buffer while freeze thaw method yielded 19.87 ± 0.43 mg g −1 CPE and 58.92 ± 3.49 mg g −1 total proteins. RSM was used to optimize phosphate buffer pH (5.5-8), molarity (0.1-1 M) and number of freeze thaw cycles (2-7). Interaction between buffer molarity and number of freeze thaw cycles was most significant for modeling the responses. Extraction of CPE was highest with pH 8 and low molarity buffers. The predicted values from the equations agreed well with the experimental values, proving the robustness of the model. The stability of the extract was also evaluated at different temperatures, light exposure times and pH values. Results indicated that light exposure should be kept to a minimum while the stability was affected by extreme temperatures and pH. CPE was comparatively stable in a pH and temperature range of 3-8 and 4-40 • C respectively.

show abstract

Section: Choice Of Buffer and Cell Disruption Methods Influence Cpe Extractionmentioning

confidence: 99%

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Ghosh

Mishra

2020

Front. Sustain. Food Syst.

View full text Add to dashboard Cite

show abstract

“…Densitometric scans were performed with a Pharmacia LKB UltroScan XL and analyzed with the Program GSXL version 2.1. The relative molar amounts of protein per band were obtained as described (31). The scaling factors used were 9.7 for L CM ; 4.5 for FNR-3D; 3.3 for L R 33 ; 2.7 for L RC 27 ; 1.8 for all PBPs; and 0.9 for L R 9 were calculated relative to six molecules of the 27-kDa L RC 27 linker polypeptide (17); the L RC 27 linkers connect the six peripheral rods of the PBS to the core.…”

Section: Methodsmentioning

confidence: 99%

“…In the cyanobacterium Synechococcus sp. PCC 7002, FNR was shown to possess a third N-terminal domain that localized the enzyme to the phycobilisomes (PBS) (), and subsequent studies similarly showed the actual mass of FNR in diverse cyanobacteria to be 45−50 kDa ( − ). With the exception of Gloeobacter violaceous PCC 7421, the predicted sequences of all cyanobacterial petH genes, encoding FNR, have lengths of 386-440 amino acids, and these sequences correspond to a protein containing three domains (here denoted FNR-3D; refs 5 , 6 , and 10−13 ).…”

mentioning

confidence: 99%

Interaction of Ferredoxin:NADP⁺Oxidoreductase with Phycobilisomes and Phycobilisome Substructures of the CyanobacteriumSynechococcussp. Strain PCC 7002

et al. 2003

View full text Add to dashboard Cite

The enzyme ferredoxin-NADP(+) oxidoreductase (FNR) from Synechococcus sp. PCC 7002 has an extended structure comprising three domains (FNR-3D) (Schluchter, W. M., and Bryant, D. A. (1992) Biochemistry 31, 3092-3102). Phycobilisome (PBS) preparations from wild-type cells contained from 1.0 to 1.6 molecules of FNR-3D per PBS, with an average value of 1.3 FNR per PBS. A maximum of two FNR-3D molecules could be specifically bound to wild-type PBS via the N-terminal, CpcD-like domain of the enzyme when exogenous recombinant FNR-3D (rFNR-3D) was added. To localize the enzyme within the PBS, the interaction of PBS and their substructures with rFNR-3D was further investigated. The binding affinity of rFNR-3D for phycocyanin (PC) hexamers, which contained a 22-kDa proteolytic fragment derived from CpcG, the L(RC)(27) linker polypeptide, was higher than its affinity for PC hexamers containing no linker protein. PBS from a cpcD3 mutant, which lacks the 9-kDa, PC-associated rod linker, incorporated up to six rFNR-3D molecules per PBS. PBS of a cpcC mutant, which has peripheral rods that contain single PC hexamers, also incorporated up to six rFNR-3D molecules per PBS. Direct competition binding experiments showed that PBS from the cpcD3 mutant bound more enzyme than PBS from the cpcC mutant. These observations support the hypothesis that the enzyme binds preferentially to the distal ends of the peripheral rods of the PBS. These data also show that the relative affinity order of the PC complexes for FNR-3D is as follows: (alpha(PC)beta(PC))(6)-L(R)(33) > (alpha(PC)beta(PC))(6)-L(RC)(27) > (alpha(PC)beta(PC))(6). The data suggest that, during the assembly of the PBS, FNR-3D could be displaced to the periphery according to its relative binding affinity for different PC subcomplexes. Thus, FNR-3D would not interfere with the light absorption and energy transfer properties of PC in the peripheral rods of the PBS. The implications of this localization of FNR within the PBS with respect to its function in cyanobacteria are discussed.

show abstract

The presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

et al. 2007

View full text Add to dashboard Cite

The complete genome sequence of Gloeobacter violaceus [Nakamura et al. (2003a, b) DNA Res 10: [37][38][39][40][41][42][43][44][45] allows us to understand better the structure of the phycobilisomes (PBS) of this cyanobacterium. Genomic analysis revealed peculiarities in these PBS: the presence of genes for two multidomain linker proteins, a core membrane linker with four repetitive sequences (REP domains), the absence of rod core linkers, two sets of phycocyanin (PC) a and b subunits, two copies of a rod PC associated linker (CpcC), and two rod cap associated linkers (CpcD). Also, there is one ferredoxin-NADP + oxidoreductase with only two domains. The PBS proteins were investigated by gel electrophoresis, amino acid sequencing and peptide mass fingerprinting (PMF). The two unique multidomain linkers contain three REP domains with high similarity and these were found to be in tandem and were separated by dissimilar Arms. One of these, with a mass of 81 kDa, is found in heavy PBS fragments rich in PC. We propose that it links six PC hexamers in two parallel rows in the rods. The other unique linker has a mass of 91 kDa and is easily released from the heavy fragments of PBS. We propose that this links the rods to the core. The presence of these multidomain linkers could explain the bundle shaped rods of the PBS. The presence of 4 REP domains in the core membrane linker protein (129 kDa) was established by PMF. This core linker may hold together 16 AP trimers of the pentacylindrical core, or alternatively, a tetracylindrical core of the PBS of G. violaceus.

show abstract

The phycobilisomes of the cyanobacterium Arthrospira (Spirulina) maxima

Cited by 12 publications

References 48 publications

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Interaction of Ferredoxin:NADP⁺Oxidoreductase with Phycobilisomes and Phycobilisome Substructures of the CyanobacteriumSynechococcussp. Strain PCC 7002

The presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

Contact Info

Product

Resources

About

The phycobilisomes of the cyanobacterium Arthrospira (Spirulina) maxima

Cited by 12 publications

References 48 publications

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Studies on Extraction and Stability of C-Phycoerythrin From a Marine Cyanobacterium

Interaction of Ferredoxin:NADP+Oxidoreductase with Phycobilisomes and Phycobilisome Substructures of the CyanobacteriumSynechococcussp. Strain PCC 7002

The presence of multidomain linkers determines the bundle-shape structure of the phycobilisome of the cyanobacterium Gloeobacter violaceus PCC 7421

Contact Info

Product

Resources

About

Interaction of Ferredoxin:NADP⁺Oxidoreductase with Phycobilisomes and Phycobilisome Substructures of the CyanobacteriumSynechococcussp. Strain PCC 7002