Cloning of the β‐phycocyanin gene from <i>Anacystis nidulans</i>

Lind, Lisbet K.; Kalla, Shubhangi; Lönneborg, Anders; Öquist, Gunnar; Gustafsson, Petter

doi:10.1016/0014-5793(85)80868-1

Cited by 23 publications

(4 citation statements)

References 20 publications

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“…The transformed mutant colonies were grown on selective plates by restreaking the colonies once a week for two months, after which the mutants were analysed by Southern blotting [22]. The D N A for Southern blotting was isolated as described by Lind et al [17]. The internal psbA (BstEII fragment of psbAI gene) and pUC18 region of the pTTQ 18 plasmid containing the integration site were used as probes.…”

Section: Construction Of the Psbaiii Over-expression Strainmentioning

confidence: 99%

Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II

et al. 1996

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Over-expression of the psbAIII gene encoding for the D1 protein (form II; D1:2) of the photosystem II reaction centre in the Synechococcus sp. PCC 7942 was studied using a tac promoter and the lacIQ system. Over-expression was induced with 40 microgram/ml IPTG in the growth medium for either 6 or 12 h at growth irradiance (50 mumol photons m-2 s-1). This treatment doubled the amount of psbAII/III mRNA and the D1:2 protein in membranes but decreased the amount of psbAI messages and the D1:1 protein. The total amount of both heterodimeric reaction centre proteins, D1 and D2, remained constant under growth light conditions, indicating that the number of PSII centres in the membranes was not affected, only the form of the D1 protein was changed from D1:1 to D1:2 in most centres. When the cells were photoinhibited either at 500 or 1000 mumol photons m-2 s-1, in the presence or absence of the protein synthesis inhibitor lincomycin, the D1:2 protein remained at a higher level in cells in which over-expression had been induced by IPTG. These cells were also less prone to photoinhibition of PSII. It is suggested that the tolerance of cells to photoinhibition increases when most PSII reaction centres contain the D1:2 protein at the beginning of high irradiance. This tolerance is further strengthened by maintaining psbAIII gene over-expression during the photoinhibitory treatment.

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Section: Construction Of the Psbaiii Over-expression Strainmentioning

confidence: 99%

Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II

et al. 1996

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“…Within the past three years many genes encoding phycobiliprotein subunits and linker polypeptides have been isolated from both cyanobacteria (Bryant et al, 1985a,c;Conley et al, 1985;Conley et al, 1986;de Lorimier et al, 1984;Lind et al, 1985;Pilot and Fox, 1984) and eukaryotic algae (Bryant et al, 1985b,c;Lemaux and Grossman, 1984;Lemaux and Grossman, 1985). Two different approaches were used in the initial isolations of phycobiliprotein genes.…”

Section: Gene Isolationmentioning

confidence: 99%

Regulated Synthesis of Phycobilisome Components

Grossman

Lemaux

Conley

1986

Photochem & Photobiology

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“…The majority of genes encoding the structural components of phycobilisomes from a number of organisms have been cloned and sequenced (Anderson & Grossman, 1987, 1989aBelknap & Haselkorn, 1987;Bryant et al, 1985aBryant et al, ,b,c, 1987Bryant et al, , 1989Conley, Lemaux & Grossman, 1985Conley et al, 1986;De Lorimier et al, 1984;Dubbs & Bryant, 1987;Grossman et al, 1988Grossman et al, , 1989Houmard et al, 1986Houmard et al, , 1988aKalla, Lind & Gustafsson, 1989;Lemaux & Grossman, 1984Lind et al, 1985;Lomax et al, 1987;Mazel et al, 1986;Mazel & Mariiere, 1989;Pilot & Fox, 1984;Tandeau de Marsac et al, 1988). Initially, the PC and AP genes {cpcBA and apcAB, respectively) were cloned from the plastid genome of the eukaryotic alga Cyanophora paradoxa (Bryant et al, 1985b;Lemaux & Grossman, 1984 and the cyanobacterial genome of Synechocoecus sp.…”

Section: Isolation Of Genes Encoding Phycobilisome Componentsmentioning

confidence: 99%

Chromatic adaptation and the events involved in phycobilisome biosynthesis

Grossman

1990

Plant Cell & Environment

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Abstract. The major light‐harvesting complex in cyanobacteria and red algae is the phycobilisome, a macromolecular complex that is attached to the surface of the photosynthetic membranes. The phycobilisome is composed of a number of different chromophoric polypeptides called phycobiliproteins and nonchromophoric polypeptides called linker proteins. Several environmental parameters modulate the synthesis, assembly and degradation of phycobilisome components. In many cyanobacteria, the composition of the phycobilisome can change to accommodate the prevalent wavelengths of light in the environment. This phenomenon is called complementary chromatic adaptation. Organisms that exhibit complementary chromatic adaptation must perceive the wavelengths of light in the environment and transduce the light signals into a sequence of biochemical events that result in altering the activities of genes encoding specific phycobiliprotein and linker polypeptides. Other environmental parameters such as light intensity and nutrient status can also have marked effects on both the number and composition of the phycobilisomes. The major concern of this article is the molecular events involved in chromatic adaptation. Most of the information concerning this process has been gained from studies involving the filamentous cyanobacterium Fremyella diplosiphon. However, also briefly considered are some of the complexities involved in phycobilisome biosynthesis and degradation; they include post‐translational modification of phycobilisome polypeptides, the coordinate expression of chromophore and apobiliprotein, the specific degradation of phycobilisomes when cyanobacteria are deprived of macronutrients such as nitrogen, sulphur and phosphorus, and the assembly of the individual phycobilisome components into substructures of the light harvesting complex.

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Cloning of the β‐phycocyanin gene from Anacystis nidulans

Cited by 23 publications

References 20 publications

Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II

Over-production of the D1:2 protein makes Synechococcus cells more tolerant to photoinhibition of photosystem II

Regulated Synthesis of Phycobilisome Components

Chromatic adaptation and the events involved in phycobilisome biosynthesis

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