Comparison of the biliproteins from two strains of the thermophilic cyanophyte <i>Synechococcus lividus</i>

MacColl, Robert; Edwards, Mercedes R.; Mulks, Martha H.; Berns, Donald S.

doi:10.1042/bj1410419

Cited by 31 publications

(20 citation statements)

References 36 publications

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“…C-phycocyanin from S. lividus that grows at the highest temperature and at pH 6.0 is entirely composed of twodisk aggregates (MacColl et al 1974). This suggested that the C-phycocyanin rods, which are C-phycocyanin-linker complexes, from the thermophilic alga are much more stable to dissociation than mesophilic C-phycocyanin rods.…”

Section: Synechococcus Lividusmentioning

confidence: 97%

Biliproteins and phycobilisomes from cyanobacteria and red algae at the extremes of habitat

Samsonoff

MacColl

2001

Archives of Microbiology

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This review considers the properties of biliproteins from cyanobacteria and red algae that grow in extreme habitats. Three situations are presented: cyanobacteria that grow at high temperatures; a red alga that grows in acidic conditions at high temperature; and an Antarctic red alga that grows in the cold in dim light conditions. In particular, the properties of their biliproteins are compared to those from organisms from more usual environments. C-phycocyanins from two cyanobacteria able to grow at high temperatures are found to differ in their stabilities when compared to C-phycocyanin from mesophilic algae. They differ in opposite ways, however. One is more stable to dissociation than the mesophilic protein, and the other is more easily dissociated at low temperatures. The thermophilic proteins resist thermal denaturation much better than the mesophilic proteins. The most thermophilic cyanobacterium has a C-phycocyanin with a unique blue-shifted absorption maximum which does not appear to be part of the adaptation of the cyanobacterium to high temperature. The C-phycocyanin from the high-temperature red alga is able to resist dissociation better than mesophilic C-phycocyanins. Electron micrographs show the phycobilisomes of these algae. The Antarctic alga grows under ice at some distance down the water column. Its R-phycoerythrin has a novel absorption spectrum that gives the alga an improved ability to harvest blue light. This may enhance its survival in its light-deprived habitat.

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Section: Synechococcus Lividusmentioning

confidence: 97%

Biliproteins and phycobilisomes from cyanobacteria and red algae at the extremes of habitat

Samsonoff

MacColl

2001

Archives of Microbiology

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“…Aggregates larger than lIS hexamer were first irreversibly disaggregated to I IS and 6S at alkaline pH (19,20 (1,20) also show a predominance of llS species near the isoelectric point and an increase of 6S species at higher pH. The reversible equilibrium of 6S and 11S species from both mesophilic and thermophilic algal sources has also been noted (1,2,15,19).…”

Section: C-mentioning

confidence: 89%

“…2). The isoelectric points of other C-phycocyanins determined using similar conditions are: C. caldarium 5.11 (15), Coccochloris elabens 4.6 (14), and Synechococcus lividus (strain I) 5.0 (19).…”

Section: C-mentioning

confidence: 98%

“…Thermophilic and mesophilic also share similarities in these same parameters but vary strikingly in the strength of their protein-protein interactions (2,13,15,16,19).…”

Section: C-mentioning

confidence: 99%

“…For thermophilic protein (2,13,16,19) this ratio is usually radically altered in either direction. Thus, one of the basic questions posed by this study is clearly resolved and this psychrophilic protein is not required to modify its aggregation properties from those of the mesophiles.…”

Section: C-mentioning

confidence: 99%

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Psychrophile C-Phycocyanin

Adams¹,

Kao²,

Berns³

1979

Plant Physiol.

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C-Phycocyanin was purified from an alga isolated in the Antarctic in 1968 and grown since that time in our laboratory at 4 C. Certain of its spectroscopic and immunochemical properties were studied, along with detailed examinations of its chemical composition and quaternary structure. The hexamer-trmer equilibrium in the protein solution was studied as a function of pH, ionic strength, temperature, and susceptibility to certain small molecules. A major emphasis of the work was placed on a comparison of its protein-protein interactions with those of C-phycocyanins from both mesophilic and thermophilk algae.The chromoprotein C-phycocyanin, an accessory photosynthetic pigment found in blue-green and red algae, has been examined in this laboratory from a variety of algal species that grow at extremes of temperature, salinity, and acidity (2, 13-16, 18, 19). In particular, C-phycocyanin isolated from thermotolerant organisms has been studied in an effort to understand what modifications in phycocyanin structure could occur at the molecular level to adjust to this environmental extreme. Sedimentation velocity experiments have shown the interesting result that the aggregation of this protein is saliently changed when mesophilic and thermophilic C-phycocyanins are compared. To have a more complete view of this concept, it is desirable to obtain data on algae that thrive in very cold environments. Will such C-phycocyanin behave as those from the higher temperature organisms and display peculiar aggregation, or will the needs of life in the cold require no changes in these parameters?To determine whether survival at low temperature has an influence on protein properties, we report in the present work observations on aggregation behavior, amino acid composition, subunit structure, isoelectric point, absorption, fluorescence, and circular dichroism spectra, and immunochemical properties of Cphycocyanin isolated from the psychrophilic blue-green alga, Microcoleus vaginatus. These findings will be compared with those for C-phycocyanin from mesophilic and thermophilic algae. The general problem of biological adaptation to cold has been reviewed (7,12) (9) for carbohydrate. Allophycocyanin and phycoerythrin were also purified by ammonium sulfate fractionation from this alga. In general, the phycoerythrin precipitated with lower and allophycocyanin with higher ammonium sulfate concentrations than C-phycocyanin. Isoelectric focusing was performed on the 110 ml LKB Ampholine column (8101) with a sucrose gradient as a stabilizing system.The amino acid analysis employed the method of Spackman et al. (23) with 6 N HCI hydrolysis at 110 C. An analysis was also performed with 4 N methanesulfonic acid hydrolysis at 110 C for 22 h to ascertain the presence of tryptophan (22).Fluorescence spectra were obtained with a Baird-Atomic fluorescence spectrophotometer SF-1 at room temperature (23 C). An RCA model 4832 photomultiplier was used since its spectral response did not change significantly over the region 300 to 800 nm. The A i...

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