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F X Cunningham

Publications and source records attributed to F X Cunningham.

23 records · Page 2Linked to original sources
PubMed1989

Stoichiometry of Photosystem I, Photosystem II, and Phycobilisomes in the Red Alga Porphyridium cruentum as a Function of Growth Irradiance.

Cells of the red alga Porphyridium cruentum (ATCC 50161) exposed to increasing growth irradiance exhibited up to a three-fold reduction in photosystems I and II (PSI and PSII) and phycobilisomes but little change in the relative numbers of these components. Batch cultures of P. cruentum were grown under four photon flux densities of continuous white light; 6 (low light, LL), 35 (medium light, ML), 180 (high light, HL), and 280 (very high light, VHL) microeinsteins per square meter per second and sampled in the exponential phase of growth. Ratios of PSII to PSI ranged between 0.43 and 0.54. About three PSII centers per phycobilisome were found, regardless of growth irradiance. The phycoerythrin content of phycobilisomes decreased by about 25% for HL and VHL compared to LL and ML cultures. The unit sizes of PSI (chlorophyll/P(700)) and PSII (chlorophyll/Q(A)) decreased by about 20% with increase in photon flux density from 6 to 280 microeinsteins per square meter per second. A threefold reduction in cell content of chlorophyll at the higher photon flux densities was accompanied by a twofold reduction in beta-carotene, and a drastic reduction in thylakoid membrane area. Cell content of zeaxanthin, the major carotenoid in P. cruentum, did not vary with growth irradiance, suggesting a role other than light-harvesting. HL cultures had a growth rate twice that of ML, eight times that of LL, and slightly greater than that of VHL cultures. Cell volume increased threefold from LL to VHL, but volume of the single chloroplast did not change. From this study it is evident that a relatively fixed stoichiometry of PSI, PSII, and phycobilisomes is maintained in the photosynthetic apparatus of this red alga over a wide range of growth irradiance.

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PubMed1988

N-terminus conservation in the terminal pigment of phycobilisomes from a prokaryotic and eukaryotic alga.

High molecular weight polypeptides from phycobilisomes, believed to be involved in facilitating the energy flow from phycobilisomes to thylakoids, are conserved in the prokaryote Nostoc sp. and the eukaryote Porphyridium cruentum. Partial N-terminal sequence analysis of the phycobilisome-polypeptides of Nostoc (94 kilodalton) and Porphyridium (92 kilodalton) revealed 55% identity in the first 20 residues, but no significant homology with sequences of other phycobiliproteins or phycobilisome-linkers. Polypeptides (94 and 92 kilodalton) from Nostoc thylakoids free of phycobilisomes, previously presumed to be involved in the phycobilisome-thylakoid linkage (M Mimuro, CA Lipschultz, E Gantt 1986 Biochim Biophys Acta 852: 126) exhibit the same immunocrossreactivity but are different from the 94 kilodalton-phycobilisome polypeptide by having blocked N-termini and a different amino acid composition.

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PubMed1986

Chlorophyll-Protein Complexes from Euglena gracilis and Mutants Deficient in Chlorophyll b: I. Pigment Composition.

The use of n-octyl-beta-d-glucopyranoside along with sodium dodecyl sulfate improves the retention of chlorophyll (Chl) by chlorophyll-protein complexes (CPs) prepared from thylakoids of Euglena gracilis Klebs var bacillaris Cori and yields several additional complexes. Thylakoids from wild-type (WT) cells, solubilized in these detergents and subjected to polyacrylamide gel electrophoresis at 0 degrees C, yield the following CPs, in order of relative molecular weight, containing the pigments shown in parentheses with their respective molar ratios where determined: CP Ia (Chl a, diadinoxanthin and beta-carotene; 100:12:5); CP I (Chl a and beta-carotene; 100:6-12); CPx (Chl and carotenoids); LHCP(2) (light-harvesting CP oligomer) (Chl a, Chl b, diadinoxanthin and neoxanthin; 12:4:3:1); CPy (Chl a, diadinoxanthin and beta-carotene; 100:14:8); CPa (Chl a and beta-carotene; 100:18-25) and LHCP (monomer) (Chl a, Chl b, diadinoxanthin and neoxanthin; 12:6:4:1). The LHCP complexes retain up to 40% of the total Chl and 80% of the Chl b in the thylakoids. CP Ia contains only a trace of Chl b (Chl a/b [mol/mol] = 62). The lower amount of Chl b in Euglena (about 10% of Chl a + b) compared to higher plants (about 30% of Chl a + b) is probably a consequence of the lower Chl b (relative to Chl a) in the LHCPs of Euglena rather than of fewer LHCPs being present. G(1)BU, Gr(1)BSL, and O(4)BSL, mutants of bacillaris low in Chl b (1-2% of Chl a + b), lack the CP Ia, LHCP, and LHCP(2) found in wildtype (WT); G(1) and O(4) also lack CPy. The mutants contain reduced amounts of Chl a (two-thirds of WT in Gr(1) and one-third in G(1) and O(4)) and neoxanthin (20-40% of WT) but retain levels of beta-carotene and diadinoxanthin close to those in cells of WT. The CPs remaining in the mutants have pigment compositions very similar to their counterparts from WT.

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PubMed1986

Chlorophyll-Protein Complexes from Euglena gracilis and Mutants Deficient in Chlorophyll b: II. Polypeptide Composition.

Chlorophyll-protein complexes (CPs) obtained from thylakoids of Euglena gracilis Klebs var bacillaris Cori contain the following polypeptides (listed in parentheses in order of prominence after Coomassie R-250 staining of polyacrylamide gels): CP Ia (66, 18, 22, 22.5, 27.5, 21, 28, 24, 25.5, and 26 kilodaltons [kD]); CP I (66 kD); CPx (41 kD); LHCP(2) (an oligomer of LHCP) (26.5, 28, and 26 kD); CPy (27 and 19 kD); CPa (54 kD); and LHCP (26.5, 28, and 26 kD). Mutants of bacillaris low in chlorophyll b (Gr(1)BSL, G(1)BU, and O(4)BSL; Chl a/b [mol/mol] = 50-100) which lack CP Ia, LHCP(2), and LHCP also lack or are deficient in polypeptides associated with these complexes in wild-type cells. Mutants G(1) and O(4), which also lack CPy, lack the CPy-associated polypeptides found in wild-type and Gr(1). Using an antiserum which was elicited by and reacts strongly and selectively with the SDS-treated major polypeptide (26.5 kD) of the LHCP complexes of wild-type, this polypeptide is undetectable in the mutants (<<0.25% of the level in wild-type on a cell basis); the antiserum does not react with the SDS-treated 28 kD polypeptide of the Euglena LHCP complexes and cross-reacts only very weakly with components in SDS-treated cells of Chlamydomonas reinhardtii Dangeard and chloroplasts of Spinacia oleracea L. cv Winter Bloomsdale. Rates of photosynthesis of the wild-type and mutant cells of Euglena are approximately equal on a cell basis when measured at light saturation, consistent with the selective loss of major antenna components but not CP I or CPa from the mutants.

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