Mastigocladus Laminosus Research Articles

The complete amino acid sequence of both subunits of allophycocyanin, a light harvesting protein-pigment complex from the cyanobacterium Mastigocladus laminosus.

The amino acid sequences of the alpha- and beta-subunit of allophycocyanin, a water-soluble light-harvesting protein-pigment complex from the thermophilic cyanobacterium Mastigocladus laminosus have been determined. The alpha-chain consists of 160 amino acid residues and the beta-chain of 161 amino acid residues. The homology of the alpha- and beta-chains is 37%. A comparison with C-phycocyanin reveals that the second chromophore of the C-phycocyanin beta-subunit is attached to an inserted peptide of 10 amino acid residues at position 151-160.

DISTRIBUTION AND PHYSIOLOGICAL DETERMINANTS OF BLUE‐GREEN ALGAL NITROGEN FIXATION ALONG A THERMOGRADIENT1

ABSTRACTThe capacity of thermal algal‐bacterial mats to fix nitrogen (N2) was examined in an alkaline thermal stream, Rabbit Creek, of Yellowstone National Park. Nitrogenase activity and nitrogen‐fixation rates of mat cores placed in serum bottles and incubated in situ were estimated by the acetylene‐reduction technique. Active nitrogenase was not detected at 60 or 65 C in either the blue‐green algal or bacterial undermat components of the mats. Acetylene was reduced by all mats ≤55 C along the thermogradient; mean fixation estimates for the mats ranged from 7 to 5,028 nmoles N2 fixed · mg Chl a−1· hr−1. Maximum fixation occurred at 35 C in the stream; statistical comparison of mean rates ordered the thermogradient mats according to estimated activities: 35 > 40 > 30 > 50 ≥ 55 ≥ 45 C. Mats (≤40 C) dominated by species of Calothrix accounted for ca. 97% of the total nitrogen fixation observed in the stream; the remaining activity was associated with mats containing Mastigocladus laminosus Cohn. Light intensity significantly affected fixation rates of the Calothrix mats which responded in a linear fashion from 9–100% full sunlight (ca. 1,900 μEin · m−2· sec−1). Calothrix mats from 30 and 40 C had maximum nitrogenase activity at their growth temperature suggesting that nitrogen fixation along the thermogradient was optimally adapted to in situ temperatures.

“Living electrode” as a long-lived photoconverter for biophotolysis of water

Living blue-green algae (Mastigocladus laminosus), immobilized on an SnO(2) optically transparent electrode with calcium alginate, functioned as an anodic photoelectrode on continuous illumination for periods of time adequate for use in a conventional electrochemical cell. This "living electrode" shows promise of use as a long-lived photoconverter of solar radiant energy to electric energy and as a suitable replacement for unstable chloroplast systems.

Photosynthetic activities of a membrane preparation of the thermophilic cyanobacterium Mastigocladus laminosus

Photosynthetically active membranes have been prepared from the thermophilic cyanobacterium Mastigogladus laminosus by treatment with lysozyme. The membranes were active in electron transport through photosystem I and II as well as in photophosphorylation and proton uptake. Cells were grown at 40°, 45° and 55°C respectively. The temperature optimum of oxygen evolution of whole cells was about 10°C higher than the growth temperature. In isolated membranes the temperature optimum for cyclic photophosphorylation was identical to the growth temperature of the cells whereas the optimum for photosystem II electron transport never exceeded 40°C. Photophosphorylation was inhibited by N, N′-dicyclohexyl carbodiimide (DCCD), carbonyl-cyanide-m-chlorophenylhydrazone and NH4Cl, whereas proton uptake was enhanced by DCCD. Electron transport was slightly inhibited by these treatments. The membranes could be stored for several weeks at-20°C in 50% glycerol without any loss in the activities.

Hydrogen Production by the Thermophilic Alga Mastigocladus laminosus : Effects of Nitrogen, Temperature, and Inhibition of Photosynthesis

Hydrogen production by nitrogen-limited cultures of a thermophilic blue-green alga (cyanobacterium), Mastigocladus laminosus, was studied to develop the concept of a high-temperature biophotolysis system. Biophotolytic production of hydrogen by solar radiation was also demonstrated. Hydrogen consumption activity in these cultures was relatively high and is the present limiting factor on both the net rate and duration of hydrogen production.

Properties of allophycocyanin II and its alpha- and beta-subunits from the thermophilic blue--green alga Mastigocladus laminosus.

Purified allophycocyanin II and its subunits have been examined with respect to spectroscopic properties, sedimentation, reconstitution and isoelectric behaviour. In 0.02m-potassium phosphate buffer, pH8.0, and at a concentration of 0.25mg/ml, allophycocyanin II and its alpha- and beta-subunits show visible absorption maxima at 650, 615 and 615nm respectively, whereas the fluorescence emission maxima were determined to be at 662, 640 and 630nm respectively. The absorption difference spectrum (dilution difference) of allophycocyanin II displays maxima at 650 and 590nm with a minimum at 610nm. The c.d. spectrum of allophycocyanin II showed only one positive-ellipticity band at 635nm, and a major negative-ellipticity band at 340nm. Oxidation of allophycocyanin II, low- and high-pH solutions (pH3.0 and 11.0), various ethanol concentrations as well as dialysis against distilled water induce a spectral change leading to phycocyanin-like characteristics. In most cases these shifts are reversible. Allophycocyanin II is thermostable over a period of 60min at temperatures up to 60 degrees C. The isoelectric points of allophycocyanin II and its alpha- and beta-subunits are 4.65, 4.64 and 4.82 respectively. Estimated molecular weights from sedimentation-equilibrium analyses were 102500 for allophycocycanin II, 16000 for the alpha- and 31500 for the beta-subunit. Recombination of alpha- and beta-subunits leads to allophycocyanin II, which is indistinguishable from native allophycocyanin with respect to its spectral form, to its gel-filtration and to its electrophoretic behaviour.

Isolation and characterization of a coupling factor I ATPase of the thermophilic blue-green alga (cyanobacterium) Mastigocladus laminosus

FEBS LettersVolume 104, Issue 1 p. 66-70 Full-length articleFree Access Isolation and characterization of a coupling factor I ATPase of the thermophilic blue-green alga (cyanobacterium) Mastigocladus laminosus Andres Binder, Andres Binder Institut für Pflanzenbiologie, Universität Zürich, Zollikerstr. 107, CH-8008 Zürich, SwitzerlandSearch for more papers by this authorReinhard Bachofen, Reinhard Bachofen Institut für Pflanzenbiologie, Universität Zürich, Zollikerstr. 107, CH-8008 Zürich, SwitzerlandSearch for more papers by this author Andres Binder, Andres Binder Institut für Pflanzenbiologie, Universität Zürich, Zollikerstr. 107, CH-8008 Zürich, SwitzerlandSearch for more papers by this authorReinhard Bachofen, Reinhard Bachofen Institut für Pflanzenbiologie, Universität Zürich, Zollikerstr. 107, CH-8008 Zürich, SwitzerlandSearch for more papers by this author First published: August 01, 1979 https://doi.org/10.1016/0014-5793(79)81086-8Citations: 40AboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL References 1 M.W.E. Pullman, H.S. Penefsky, A. Datta, E. Racker, J. Biol. Chem., 235, (1960), 3322– 3329. 2 F.M. Harold, Curr. Top. Bioenerg., 6, (1977), 83– 91. 3 N. Sone, M. Yoshida, H. Hirata, Y. Kagawa, J. Biol. Chem., 252, (1977), 2956– 2960. 4 N. Nelson, Biochim. Biophys. Acta, 456, (1976), 314– 338. 5 B.C. Johansson, M. Baltscheffsky, H. Baltscheffky, A. Baccarini-Melandri, B.A. Melandri, Eur. J. Biochem., 40, (1973), 109– 117. 6 A. Binder, E. Tel-Or, M. Avron, Eur. J. Biochem., 67, (1976), 187– 196. 7 Bohler, M. C. and Binder, A. (1979) submitted. 8 A. Binder, P. Locher, H. Zuber, Arch. Hydrobiol., 70, (1972), 541– 555. 9 R.W. Castenholz, Bact. Rev., 33, (1969), 576– 594. 10 B.R. Beechey, S.A. Hubbard, P.E. Linnett, E.A. Munn, Biochem. J., 148, (1975), 533– 537. 11 A. Binder, A. Jagendorf, E. Ngo, J. Biol. Chem., 253, (1978), 3094– 3100. 12 H.H. Taussky, E. Shorr, J. Biol. Chem., 202, (1953), 675– 685. 13 O.H. Lowry, N.J. Rosebrough, A.L. Farr, R.J. Randall, J. Biol. Chem., 193, (1951), 265– 275. 14 A. Bensadun, D. Weinstein, Anal. Biochem., 70, (1976), 241– 250. 15 G. McKinney, J. Biol. Chem., 140, (1941), 315– 321. 16 U.K. Laemmli, Nature, 227, (1970), 680– 685. 17 M.H. Younis, G.D. Winget, E. Racker, J. Biol. Chem., 252, (1977), 1814– 1818. 18 S. Lien, E. Racker, Methods Enzymol., 23, (1971), 547– 555. Citing Literature Volume104, Issue1August 01, 1979Pages 66-70 ReferencesRelatedInformation

The amino acid sequence of ferredoxin from the alga Mastigocladuslaminosus

Ferredoxin was purified from the thermophilic blue-green alga, Mastigocladus laminosus. The physicochemical properties of this ferredoxin are similar to those of other [2Fe-2S] plant ferredoxins except for its unusual thermal stability. The primary structure of the protein was determined and consists of 98 amino acid residues, 5 of which are cysteines. The positions of 4 cysteines which bind the iron atoms of the active centre are identical to those in other ferredoxins. The primary structure of the ferredoxin does not reveal any special features to account for its high thermal stability.

The complete amino acid sequence of both subunits of C-phycocyanin from the cyanobacterium Mastigocladus laminosus.

The amino acid sequences of both subunits of the C-phycocyanin from the thermophilic cyanobacterium Mastigocladus laminosus have been determined. The alpha-chain consists of 162 amino acid residues and has a molecular weight of 18000, whereas the beta-chain consists of 172 residues and has a molecular weight of 19400. For the first three quarters of their length the polypeptide chains are 31% homologous, whereas there is no significant homology in the final quarter up to the C-terminus. This could mean that the introduction of an additional chromophore binding site in the last quarter of the beta-chain during evolution was achieved via a large number of point mutations or by exchange of the whole C-terminal part in an ancestral gene.

Similar C-phycocyanins from two strains of thermotolerant cyanophyte Mastigocladus laminosus

C-phycocyanin from two strains of the thermotolerant blue-green alga, Mastigocladus laminosus (NZ-DB2-m and I-30-m), that grow within different temperature ranges have been characterized with respect to aggregation, immunologic properties, subunit composition, and thermodenaturation. The critical thermal-denaturation temperature for phycocyanin from both strains of M. laminosus phycocyanin is 60 degrees C which is higher than that for mesophilic phyococyanin. Immunodiffusion studied have shown that these two strains of M. laminosus exhibit no antigenic differences and are closely related to the mesophilic Plectonema calothricoides and the thermophilic Synechococcus lividus (strains 3). Neither phenol nor alpha-naphthol has any effect on phycocyanin aggregation in these two strains of M. laminosus. There is also no enhancement of formation of large aggregates at their elevated temperature of cultivation. Furthermore, the phycocyanin of both strains of M. laminosus does not demonstrate any large amount of 19S or higher aggregates at any pH value. These observations suggest that the mode of adaptation of M. laminosus phycocyanin to high temperature is differnet from the previously encountered. It is also important to note that phycocyanin is essentially unchanged whether it is extracted from the same strain, M. laminosus (NZ-DBS-m), grown at either 50 degrees C or 37 degrees C.

Allophycocyanin I—A second cyanobacterial allophycocyanin? isolation, characterization and comparison with allophycocyanin II from the same alga

In addition to chlorophyll and carotinoids bluegreen algae contain phycocyanin, allophycocyanin and frequently phycoerythrin [ 1,2] . Action spectra for photosynthetic oxygen evolution and for the excitation of chlorophyll a fluorescence demonstrate that the phycobiliproteins function as accessory pigments [3,4]. Generally it has been assumed that the energy absorbed by phycoerythrin is passed via phycocyanin to chlorophyll a [5-71. The role played by allophycocyanin has remained unclear mainly because of its low concentration in the cell and since its major absorption band (650 nm) is masked by those of phycocyanin and chlorophyll a. Recently it has been demonstrated for intact phycobilisomes from red [8] and blue-green algae [9] that excitation with light absorbed by phycoerythrin ieads to a fluorescence of a much longer wavelength than that emitted by phycocyanin. This means that the energy is transferred from phycoerythrin through phycocyanin to allophyce cyanin. The last-named compound seems to be the key pigment from which the energy is passed to chlorophyll a with high efficiency. During our studies of biliproteins from the blue-green alga Mastigocladus laminosus [ 10,l l] we observed the presence of very small amounts of an undescribed biliprotein with an absorption spectrum resembling that of allophycocyanin. According to its early elution

THE EFFECT OF SULFIDE ON THE BLUEGREEN ALGAE OF HOT SPRINGS. I. NEW ZEALAND AND ICELAND1

SUMMARYThe concentration of soluble sulfide (H2S, HS−, S=)2 in hot springs of New Zealand and Iceland has a “species‐determining” effect which appears to override the effect of all other chemical factors excepting hydrogen ion concentration. The cosmopolitan high‐temperature form (HTF) of Mastigocladus laminosus (Ag.) Cohn appears to be sensitive to concentrations of S= over 0.15 mg·l−1 in New Zealand and 0.25 mg·l−1 in Iceland. It was absent in thermal streams where S= level was high enough to exceed this concentration at a point below its optimal temperature range (i.e., below ca. 50 C). In low or non‐S= springs in these regions this alga formed mats to an upper temperature limit of 63–64 C.In contrast, one bluegreen alga (Oscillatoria amphigranulata van Goor) occurred abundantly only in moderate to high S= springs of New Zealand; this was a species with an upper temperature limit of about 57 C. Field 14C‐HCO3− incorporation experiments with various levels of added S= confirmed the sensitivity of HTF Mastigocladus and the great tolerance of O. amphigranulata. In the latter, the photosynthetic incorporation of 14C‐HCO3− was sustained or enhanced by the additions of S= in the presence of 5 × 10−5m DCMU, an inhibitor of photoelectron transport on the reducing side of photosystem II. It is possible, but not proven, that S= may act as a photoreductant in this species.

Isolation and characterization of allophycocyanin II from the thermophilic blue-green alga Mastigocladus laminosus cohn

Isolation and characterization of allophycocyanin II from the thermophilic blue-green alga Mastigocladus laminosus cohn

A Solid State pH Control System for Algal Culturing and Uptake Studies

An inexpensive solid state pH control circuit was built for external use with existing pH meters that can use either a gas or a liquid solution for pH control of culture media. Mastigocladus laminosus showed a 49% reduction in the rate of radiophosphate (P—32) uptake between gas—controlled (30% CO2 in air) pH intervals of 8.7 (optimal uptake) and 5.7. Isotope uptake rates at higher pH values (achieved by manual additions of 0.1 N NaOH) decreased slightly between pH 8.7 and 9.7 and declined 36% between 9.7 and 10.7, where trichome motility and the ability to colonize new substratum were inhibited. Suppression of growth based on short—term (96 hr) dry weights, of which only 24 hr were at the selected pH values, was not evident throughout the experimental pH range.

Patterns of radiocarbon uptake by a thermophilic blue‐green alga under varying conditions of incubation

Current‐enhanced uptake of radiocarbon by Mastigocladus laminosus Cohn was demonstrated in a laboratory stream using in situ (current flow at 40 cm sec−1 vs. 1–3 cm sec−1) and in vitro (incubation in a vial) techniques. Isotope profiles through in situ cores showed high surface incorporation. Measurements made using the in vitro technique of incubation approached results obtained under natural flow, but may be an artifact of the technique.

Chromophore-containing peptide sequences in C-phycocyanin from Mastigocladus laminosus

Chromophore-containing peptide sequences in C-phycocyanin from Mastigocladus laminosus

C-phycocyanin from the thermophilic blue-green alga Mastigocladus laminosus, isolation, characterization and subunit composition

C-phycocyanin from the thermophilic blue-green alga Mastigocladus laminosus, isolation, characterization and subunit composition

Microbiological studies of thermal habitats of the central volcanic region, North Island, New Zealand

Abstract This account of studies on the algae and bacteria of North Island thermal areas records temperature, pH and species found in these microbial habitats, with special attention to organisms living at the highest temperatures. Thermal features were studied at Rotorua (Whakarewarewa and Ohinemutu), Waiotapu (Tourist Reserve and Lady Knox Geyser), Orakei Korako, Taupo Spa, Waikite Springs, Wairakei thermal valley, Wairakei geothermal field, Tikitere, Ketetahi, Lake Rotokawa (Taupo region), Waimangu, De Brett Thermal Hotel (Taupo). The upper temperature limit for blue‐green algae in New Zealand is 60–65°c, and the species living at the thermal limit is generally Mastigocladus laminosus, although in some cases Phormidium sp. or Synechococcus sp. was found. The Synechococcus sp. characteristic of high temperatures (73–74°c) present in North America was not found in New Zealand. In virtually all boiling pools (99–101°c) with pH values in the neutral and alkaline range bacteria were found, but in acidic boi...

THE ALGAE OF WAIMANGU CAULDRON (NEW ZEALAND): DISTRIBUTION IN RELATION TO pH1

SUMMARYThe pH of the main body of thermal water and of the outlet of Waimangu Cauldron (Frying Pan Lake) is 3.8, whereas hot springs flowing into this lake are alkaline, pH 8.2–8.7. Where these waters meet there are pH gradients, and it is possible to find a series of habitats differing in pH but having approximately the same temperature (54–56 C). Where the pH is above 4.8 the blue‐green alga Mastigocladus laminosus is present, and where the pH is below this value the eucaryotic alga Cyanidium caldarium is the sole photosynthetic microorganism at temperatures less than 55 C. Rocks resting on the bottom of Waimangu Cauldron surrounded by water of pH 3.8 have Mastigocladus laminosus growing on them, but measurements of pH directly in these algal mats showed that the microenvironment of the alga was actually above pH 4.8. A simple experiment showed that it is probably the rock, per se, that initiates a tiny island of alkalinity in the acid lake, permitting M. laminosus to become established. The outlet of Waimangu Cauldron is a hot acid stream which becomes progressively alkaline as it descends through Waimangu Valley, due to inflow of alkaline water from springs and a cold stream. Blue‐green algae were found in this stream when the pH was greater than 5.0 and C. caldarium when the pH was less than 4.0. In one region where the pH was between 4.0 and 5.0, both blue‐green algae and C. caldarium were seen, although in moribund state. These data, provide further information on the lowest pH values at which blue‐green algae are able to grow.

THE THERMOPHILIC CYANOPHYTES OF ICELAND AND THE UPPER TEMPERATURE LIMIT(1).

The upper temperature limit for the growth of chlorophyllous cyanophytes was estimated at about 63-64 C by observations of field populations and by the growth of culture isolates at that temperature. Several isolates of Mastigocladus laminosus were made from different Iceland springs and temperatures. A few continued to grow at 62 C and one at 64 C. M. laminosus was the cyanophyte in Iceland tolerant of the highest temperature. The several species or races of narrow-cell-form Synechococcus, which almost exclusively inhabit North American and other springs above 62 C and up to about 74 C, were not found in Iceland. According to my observations and those of others, a maximum of 6-8 cyanophyte species occur in waters over 45 C in all of Iceland. Many times this number has been reported from continental regions of great thermal activity. The low number of species and the absence of particular thermophilic cyanophytes may result from inadequate dispersal from other thermal areas since the end of the last glaciation. Environmental inadequacies (e.g., winter darkness, or minimum-maximum concentrations of nutrients or other solutes) may also be factors in the absence of certain species.