Chlorina mutants of barley (Hordeum vulgare L.)

Simpson, David J. W.; Machold, O.; Høyer‐Hansen, Gunilla; Wettstein, Diter von

doi:10.1007/bf02907148

Cited by 64 publications

(39 citation statements)

References 23 publications

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“…Neoxanthin is associated with the Lhcb polypeptides (Bassi et al, 1993;Thornber et al, 1993), which are severely depleted in chlorina f2. As a consequence, neoxanthin (and of course Chl b) was largely reduced in chlorina f2 if compared to wild type, as reported by Simpson et al (1985). In plants grown in normal light, the only prominent change in pigment composition induced by the HL treatment was de-epoxidation of violaxanthin into antheraxanthin and zeaxanthin (Table IV).…”

Section: Pigment Analysissupporting

confidence: 62%

“…Typically, these plants lack the major LHC proteins, Lhcbl and Lhcb2 (Simpson et al, 1985;White and Green, 1987;Allen et al, 1988) but still contain various amounts of minor LHC proteins (White and Green, 1988;Peter and Thornber, 1991;Marquardt and Bassi, 1993;Jahns and Krause, 1994). The barley (Hordeum vulgare L.) chlorina f2 mutant (Simpson et al, 1985) is the most wellcharacterized Chl b-deficient mutant. Severa1 studies have addressed its LHC polypeptide composition Green, 1987, 1988;Morrissey et al, 1989;Harrison and Melis, 1992;Harrison et al, 1993), but it is still not fully disclosed.…”

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confidence: 99%

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Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Krol¹,

Spangfort²,

Hüner³

et al. 1995

Plant Physiol.

171

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Section: Pigment Analysissupporting

confidence: 62%

mentioning

confidence: 99%

Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Krol¹,

Spangfort²,

Hüner³

et al. 1995

Plant Physiol.

171

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“…Leaky mutants would produce lower levels of intermediates in the Chl biosynthetic pathway than those present in normal plants. Such leaky mutants for Chl biosynthesis in higher plants have been reported (7,10,13). Lowered concentrations of the intermediate just prior to the branch in pathways leading to Chl a or Chl b might perturb the final ratio of these two pigments.…”

mentioning

confidence: 89%

Chlorophyll Expression Varies with Development State in the Temperature-Sensitive ch4 Mutation of Melilotus alba

Markwell

Chelgren²

1988

Plant Physiol.

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The ch4 mutant of sweetclover (Melilotus alba) has previously been demonstrated to be temperature-and photoperiod-sensitive for the accumulation of chlorophyll. Pigment content of ch4 mutant leaves was examined as a function of trifoliolate mass, an index of leaf development. Inhibition of chlorophyll accumulation caused by increased growth temperature or decreased photoperiod can be attenuated during the earliest leaf development stages but is almost complete after the trifoliolates have reached 10 milligrams in size. Once this size is reached, the total amount of chlorophyll per trifoliolate remains constant, and the amount of chlorophyll per gram of leaf decreases as the leaf expands. We have evidence for several other sweetclover mutants with this general phenotype, all with alterations previously determined to be located in different genes as evidenced by complementation following genetic crosses. This mutant phenotype may represent lesions in the chlorophyll biosynthetic pathway or the assembly of the photosynthetic apparatus.During a recent study on nuclear mutants of sweetclover (Melilotus alba) with less than normal amounts of Chl b, it was discovered that the ch4 mutant, which is normally characterized by somewhat reduced amounts of Chl and an elevated ratio of Chl alb, was temperature-and photoperiod-sensitive (8). Growth of the plant at 23°C and 16 h photoperiod (termed a permissive condition) resulted in its usual phenotype, leaves containing about one-third the normal amount of Chl and a somewhat elevated ratio of Chl alb. However, growth at 26°C and 16 h photoperiod or at 23°C and 8 h photoperiod (termed nonpermissive conditions) resulted in production of stunted plants with yellow leaves. The effect of the mutation on plants grown under these latter conditions appeared to be relatively specific for Chl content, which was reduced over 20-fold relative to normal plants; the amount of ribulose 1,5-bisphosphate carboxylase activity, an indicator of cytoplasmic and chloroplastic protein synthesis, was only half of normal. It was suggested that the molecular basis of this mutation was some developmentally regulated process involved in pigment production.The data in this manuscript will demonstrate that the ch4 mutation appears to set limitations on RESULTSWhile studies on the temperature-sensitive nature of the ch4 sweetclover mutant were in progress, it was noticed that, whereas the large and medium-sized trifoliolates on the ch4 mutant plants grown at 26°C with 16 h photoperiod were clearly Chl deficient, the very small trifoliolates appeared to be more green in color. Consequently, the pigment content of the ch4 mutant was examined as a function of trifoliolate mass, which should be an indirect indicator of developmental state; smaller trifoliolates should generally be at an earlier developmental state than larger trifoliolates on the same plant. For comparison, the pigment content was also measured in trifoliolates of normal and ch5 mutant plants grown under identical conditions. All mat...

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“…The light-and temperature-sensitive clo f104 mutant lacks a large complement of Lhcb1 in addition to lacking the 23 kD Lhca2 protein of PS I (Knoetzel & Simpson 1991;Bossman et al 1997). These mutants were chosen for this study because they both exhibit strong variations in their PS I chlorophyll emission spectral amplitudes at 77 K and signi¢cant di¡erences in their room temperature steadystate £uorescence behaviour (Simpson et al 1985;Bassi et al 1985). It was thus of interest to determine and characterize the probable relationships between the 77 K spectral changes due to PS I and the room temperature £uorescence parameters.…”

Section: Introductionmentioning

confidence: 99%

Global spectral–kinetic analysis of room temperature chlorophyll a fluorescence from light-harvesting antenna mutants of barley

Gilmore

Itoh

Govindjee

2000

Phil. Trans. R. Soc. Lond. B

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This study presents a novel measurement, and simulation, of the time-resolved room temperature chlorophyll a £uorescence emission spectra from leaves of the barley wild-type and chlorophyll-b-de¢cient chlorina (clo) f 2 and f104 mutants. The primary data were collected with a streak-camera-based picosecond-pulsed £uorometer that simultaneously records the spectral distribution and time dependence of the £uorescence decay. A new global spectral-kinetic analysis programme method, termed the double convolution integral (DCI) method, was developed to convolve the exciting laser pulse shape with a multimodal-distributed decay pro¢le function that is again convolved with the spectral emission band amplitude functions. We report several key results obtained by the simultaneous spectral-kinetic acquisition and DCI methods. First, under conditions of dark-level £uorescence, when photosystem II (PS II) photochemistry is at a maximum at room temperature, both the clo f 2 and clo f104 mutants exhibit very similar PS II spectral-decay contours as the wild-type (wt), with the main band centred around 685 nm. Second, dark-level £uorescence is strongly in£uenced beyond 700 nm by broad emission bands from PS I, and its associated antennae proteins, which exhibit much more rapid decay kinetics and strong integrated amplitudes. In particular a 705^720 nm band is present in all three samples, with a 710 nm band predominating in the clo f 2 leaves. When the PS II photochemistry becomes inhibited, maximizing the £uorescence yield, both the clo f104 mutant and the wt exhibit lifetime increases for their major distribution modes from the minimal 250^500 ps range to the maximal 1500^2500 ps range for both the 685 nm and 740 nm bands. The clo f 2 mutant, however, exhibits several unique spectral-kinetic properties, attributed to its unique PS I antennae and thylakoid structure, indicating changes in both PS II £uorescence reabsorption and PS II to PS I energy transfer pathways compared to the wt and clo f104. Photoprotective energy dissipation mediated by the xanthophyll cycle pigments and the PsbS protein was uninhibited in the clo f 104 mutant but, as commonly reported in the literature, signi¢cantly inhibited in the clo f 2; the inhibited energy dissipation is partly attributed to its thylakoid structure and PS II to PS I energy transfer properties. It is concluded that it is imperative with steady-state £uorometers, especially for in vivo studies of PS II e¤ciency or photoprotective energy dissipation, to quantify the in£uence of the PS I spectral emission.

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Chlorina mutants of barley (Hordeum vulgare L.)

Cited by 64 publications

References 23 publications

Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Chlorophyll a/b-Binding Proteins, Pigment Conversions, and Early Light-Induced Proteins in a Chlorophyll b-less Barley Mutant

Chlorophyll Expression Varies with Development State in the Temperature-Sensitive ch4 Mutation of Melilotus alba

Global spectral–kinetic analysis of room temperature chlorophyll a fluorescence from light-harvesting antenna mutants of barley

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