Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections

Gallagher, Seán P.; Short, Timothy W.; Ray, Peter M.; Pratt, Lee H.; Briggs, Winslow R.

doi:10.1073/pnas.85.21.8003

Cited by 123 publications

(76 citation statements)

References 17 publications

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“…Grey Stripe), and zucchini (Cucurbita pepo L. cv) were grown in total darkness for 7 d as described (6), except that seeds were allowed to imbibe and were grown with one-quarter strength Hoagland solution. Stem sections (8)(9)(10) Procedures for the in vitro phosphorylation (18) and the separation and analysis of proteins by SDS-PAGE and autoradiography (6) have been described previously.…”

Section: Plant Materialsmentioning

confidence: 99%

“…4). Gallagher et al (6), studying the phosphorylation of membrane proteins extracted from etiolated pea epicotyls, discovered that light was affecting the phosphorylation of a 120-kD protein associated with the plasma membrane. Subsequently, Short et al (16,17) showed that in vitro irradiation induced a strong enhancement of the phosphorylation of a 120-kD protein in pea and a 114-kD protein in maize (10,15).…”

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confidence: 99%

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Blue Light Activates a Specific Protein Kinase in Higher Plants

Reymond

Short²,

Briggs³

1992

Plant Physiol.

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Hence, this system is probably ubiquitous in higher plants. Solubilized maize membranes exposed to blue light and added to unirradiated solubilized maize membranes show a higher level of phosphorylation of the light-affected protein than irradiated membrane proteins alone, suggesting that an unirradiated substrate is phosphorylated by a light-activated kinase. This finding is further demonstrated with membrane proteins from two different species, where the phosphorylated proteins are of different sizes and, hence, unambiguously distinguishable on gel electrophoresis. When solubilized membrane proteins from one species are irradiated and added to unirradiated membrane proteins from another species, the unirradiated protein becomes phosphorylated. These experiments indicate that the irradiated fraction can store the light signal for subsequent phosphorylation in the dark. They also support the hypothesis that light activates a specific kinase and that the systems share a close functional homology among different higher plants.Light provides plants with many different kinds of information about their environment. This information is integrated by sensory systems and used to optimize a variety of physiological and morphological processes. Different classes of responses are defined according to the region of the light spectrum that activates them. The effects of red light on

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Section: Plant Materialsmentioning

confidence: 99%

mentioning

confidence: 99%

Blue Light Activates a Specific Protein Kinase in Higher Plants

Reymond

Short²,

Briggs³

1992

Plant Physiol.

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“…Each sample normally consisted of 50 sections, and harvest of the standard eight samples (the maximum number for a given experiment) usually required less than 30 min. Since Gallagher et al ( 11) showed that red light did not affect the phosphorylation phenomenon appreciably, segments were harvested under dim red light (approximately 0.5 ,umol/m2s) at 24°C.…”

Section: Plant Materialsmentioning

confidence: 99%

“…Repetitions of a given experiment were performed with the various treatments in different sequences to minimize the effect of any post-harvest, time-dependent variable. In vitro irradiations were performed on ice with 200 .ug total protein in the phosphorylation buffer and distilled water mixture described for the phosphorylation reaction (11). The phosphorylation procedure was initiated immediately following each irradiation.…”

Section: Irradiationsmentioning

confidence: 99%

Characterization of a Rapid, Blue Light-Mediated Change in Detectable Phosphorylation of a Plasma Membrane Protein from Etiolated Pea (Pisum sativum L.) Seedlings

Short¹,

Briggs²

1990

Plant Physiol.

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102

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When crude microsomal membranes from apical stem segments of etiolated Pisum sativum L. cv Alaska are mixed in vitro with 'y-[32P]ATP, a phosphorylated band of apparent molecular mass 120 kilodaltons can be detected on autoradiographs of sodium dodecyl sulfate electrophoresis gels. If the stem sections are exposed to blue light immediately prior to membrane isolation, this band is not evident. The response is observed most strongly in membranes from the growing region of the stem, but no 120 kilodalton radiolabeled band is detected in membranes from the developing buds. Fluence-response curves for the reaction show that the system responds to blue light above about 0.3 micromole per square meter, and the visible phosphorylation completely disappears above 200 micromoles per square meter. Reciprocity is valid for the system, because varying illumination time or fluence rate give similar results. If the stem segments are left in the dark following a saturating blue irradiation, the radiolabeled band begins to return after about 10 minutes and is as intense as that from the dark controls within 45 to 60 minutes. A protein that comigrates with the phosphorylated protein on polyacrylamide gels is also undetectable after saturating blue light irradiations. The fluence range in which the protein band disappears is the same as that for the disappearance of the phosphorylation band. Its dark recovery kinetics and tissue distribution also parallel those for the phosphorylation. In vitro irradiation of the isolated membranes also results in a phosphorylation change at that molecular mass, but in the opposite direction. Comparisons of the kinetics, tissue distribution, and dark recovery of the phosphorylation response with those published for blue lightmediated phototropism or rapid growth inhibition indicate that the phosphorylation could be linked to one or both of those reactions. However, the fluence-response relationships for the change in detectable phosphorylation match quite closely those reported for phototropism but not those for growth inhibition. Blue light has also been found to regulate the capacity for in vitro phosphorylation of a second protein. It has an apparent molecular mass of 84 kilodaltons and is localized primarily in basal stem sections.

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“…The first hint toward understanding phototropism at the biochemical leve1 came when Gallagher et al (1988) described the blue light-dependent phosphorylation of a 120-kD plasma membrane-associated protein in pea. A corresponding response has subsequently been detected in a11 higher plants investigated (Reymond et al, 1992).…”

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confidence: 99%

Exposure of Oat Seedlings to Blue Light Results in Amplified Phosphorylation of the Putative Photoreceptor for Phototropism and in Higher Sensitivity of the Plants to Phototropic Stimulation

Salomon¹,

Zacherl²,

Luff³

et al. 1997

Plant Physiology

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Dark recovery of blue light-induced i n vitro phosphorylation in oat (Avena safiva L.) seedlings after in vivo preirradiation with blue light revealed different recovery kinetics for the coleoptile base and tip. Although, in both cases, maximum in vitro phosphorylation was observed 90 min after i n vivo blue light treatment, the phosphorylation levels for the entire base were about 3-fold higher than those found in nonpreirradiated plants. l h e tip response only slightly exceeded that of the dark controls. l h e fluence applied during preirradiation determined the extent of the increase in phosphorylation. Consequently, unilateral irradiation and subsequent dark incubation resulted in a more pronounced increase in phosphorylation in the irradiated than in the shaded side of the coleoptile base. Furthermore, blue light-irradiation conditions, known to induce neither first-nor second-positive curvature in nonpreirradiated plants, stimulated both asymmetric distribution of protein phosphorylation and second-positive phototropic curvature in the coleoptile base when administered to blue light-pretreated plants. Based on these data, we conclude that photosensitivity of the coleoptile base increases upon exposure to blue light i n a time-and fluence-dependent manner, providing an excellent explanation of the invalidity of the Bunsen-Roscoe reciprocity law for secondpositive phototropism.Phototropism has been studied in a variety of dicotyledoneous and monocotyledoneous plants over the last century (for reviews, see Firn and Digby, 1980;Briggs and Baskin, 1988;Iino, 1990; Firn, 1994). The most extensive studies on phototropic-curvature reactions were done on the coleoptile of etiolated oat (Avena sativa L.) seedlings, a classic object of phototropism research. From the fluenceresponse curves obtained by unilateral irradiation of oat coleoptiles with blue or white light at least three different types of bending reactions have been distinguished with respect to the light-stimulus intensity and duration (Briggs,

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Light-mediated changes in two proteins found associated with plasma membrane fractions from pea stem sections

Cited by 123 publications

References 17 publications

Blue Light Activates a Specific Protein Kinase in Higher Plants

Blue Light Activates a Specific Protein Kinase in Higher Plants

Characterization of a Rapid, Blue Light-Mediated Change in Detectable Phosphorylation of a Plasma Membrane Protein from Etiolated Pea (Pisum sativum L.) Seedlings

Exposure of Oat Seedlings to Blue Light Results in Amplified Phosphorylation of the Putative Photoreceptor for Phototropism and in Higher Sensitivity of the Plants to Phototropic Stimulation

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