scholarly journals Lysyl oxidase-like protein secreted from an acidophilic red alga, Cyanidium caldarium

Plant Direct ◽  
2018 ◽  
Vol 2 (10) ◽  
pp. e00084
Author(s):  
Tatsuya Tomo ◽  
Akinori Okumura ◽  
Takehiro Suzuki ◽  
Mirai Okuhara ◽  
Ruriko Katayama ◽  
...  
1987 ◽  
Vol 105 (2) ◽  
pp. 247-254 ◽  
Author(s):  
VITTORIA MARTINO RIGANO ◽  
VINCENZA VONA ◽  
CATELLO MARTINO ◽  
CARMELO RIGANO

1988 ◽  
Vol 254 (3) ◽  
pp. 907-910 ◽  
Author(s):  
J D Houghton ◽  
L Turner ◽  
S B Brown

Pigment synthesis in four strains of the unicellular red alga Cyanidium caldarium with different pigment-synthesizing patterns was inhibited in the presence of gabaculine (3-amino-2,3-dihydrobenzoic acid). Parallel inhibition of light-induced chlorophyll and phycocyanin synthesis was observed in strain III-D-2, which only synthesizes pigments in the light. Similar parallel inhibition was observed in the dark in mutant CPD, which is able to synthesize chlorophyll and phycocyanin in the absence of light. Inhibition of pigment synthesis in all strains was overcome by addition of 5-aminolaevulinic acid. Inhibition of phycocyanin synthesis in mutant GGB (unable to synthesize chlorophyll) and inhibition of chlorophyll synthesis in mutant III-C (unable to synthesize phycocyanin) were also observed. Gabaculine also inhibited the heterotrophic growth of C. caldarium in the dark. However, inhibition was overcome after an extended lag period, following which cell growth proceeded at a similar rate to that of control cells not exposed to gabaculine. Heterotrophic growth in cells pre-exposed to gabaculine was not inhibited by subsequent exposure. Possible mechanisms for this adaptation are discussed.


1984 ◽  
Vol 219 (3) ◽  
pp. 905-909 ◽  
Author(s):  
S B Brown ◽  
J A Holroyd ◽  
D I Vernon

14C-labelled biliverdin IX alpha was administered to cultures of Cyanidium caldarium that were actively synthesizing photosynthetic pigments in the light. Between 9 and 12% of the phycobiliprotein chromophore produced in such cultures was derived from exogenous biliverdin. These results demonstrate that biliverdin is an intermediate in the biosynthesis of phycobiliproteins.


1994 ◽  
Vol 26 (2) ◽  
pp. 136-138 ◽  
Author(s):  
Niji Ohta ◽  
Shigeyuki Kawano ◽  
Tsuneyoshi Kuroiwa

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