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Cited by 27Light effects on plantsPlant Molecular Biology ResearchPhotosynthetic Processes and Mechanisms

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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Salomon, M., Zacherl, M., Luff, L., Rudiger, W.·1997·Plant Physiology
DOI 10.1104/pp.115.2.493PMC PMC158507
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Abstract

Dark recovery of blue light-induced in vitro phosphorylation in oat (Avena sativa 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 in vivo blue light treatment, the phosphorylation levels for the entire base were about 3-fold higher than those found in nonpreirradiated plants. The tip response only slightly exceeded that of the dark controls. The 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 in a time-and fluence-dependent manner, providing an excellent explanation of the invalidity of the Bunsen-Roscoe reciprocity law for second-positive phototropism.

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  • Unilateral blue light induced autophosphorylation of PHOT1 in oat coleoptiles and exhibited a gradient distribution.

    “An early study revealed that unilateral blue light induced autophosphorylation of PHOT1 in oat (Avena sativa) coleoptiles and exhibited a gradient distribution (Salomon et al., 1997).”

    From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Salomon et al., 1997

    The Results section (page not provided) reports that unilateral blue-light irradiation produced asymmetric phosphorylation across oat coleoptiles, with higher in vivo phosphorylation on the irradiated side. But the paper calls the 116-kD protein a putative photoreceptor and does not establish in our copy that it is PHOT1 or that its phosphorylation is autophosphorylation. (LLM, conf=0.88)

    Experimental — accuracy not yet measured

  • CUL3 is required for blue light-induced ubiquitination of PHOT1, and PHOT1 ubiquitination is thought to be involved in phototropism.

    “CUL3 is required for blue light-induced ubiquitination of PHOT1, and PHOT1 ubiquitination is thought to be involved in phototropism (Salomon et al., 1997; Thomann et al., 2005; Roberts et al., 2011).”

    From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Salomon et al., 1997

    The Abstract and Discussion discuss blue light-induced phosphorylation of a putative photoreceptor and its relationship to phototropism. Searches for CUL3, PHOT1, and ubiquitination found no passage addressing whether CUL3 is required for PHOT1 ubiquitination or whether that ubiquitination is involved in phototropism; phosphorylation is a different process. (LLM, conf=0.76)

    Experimental — accuracy not yet measured

  • When the auxin reporter gene DR5rev:GFP was transferred into oat, blue light led to the formation of an auxin concentration gradient in the stem.

    “When the auxin reporter gene DR5rev:GFP was transferred into oat, blue light led to the formation of an auxin concentration gradient in the stem (Salomon et al., 1997; Zhu, 2021b).”

    From The action of enhancing weak light capture via phototropic growth and chloroplast movement in plants (2022) · cites this paper as Salomon et al., 1997

    The Plant Material section describes oat seedlings, and the Results and Discussion describe blue-light-induced gradients of 116-kD protein phosphorylation in their coleoptiles. Our copy does not describe transferring DR5rev:GFP into oat or measuring an auxin concentration gradient (searched for the reporter and auxin gradient). (LLM, conf=0.78)

    Experimental — accuracy not yet measured

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Authors
Salomon, M., Zacherl, M., Luff, L., & Rudiger, W.
Affiliations
  • Ludwig-Maximilians-Universität München (DE)
  • Botanisches Institut der Universitat Munchen, Menzinger Strasse 67, D-80638 Munchen, Germany
ORCID
Salomon, M.
Venue
Plant Physiology
Publisher
Oxford University Press (OUP)
Published
1997-10-01
Volume
115
Issue
2
Pages
493-500
ISSN
  • 0032-0889 (ISSN-L)
  • 1532-2548
DOI
10.1104/pp.115.2.493
PMC
PMC158507
OpenAlex
W1767296809
Cited by
27
References
26
Citations by year
2022: 1 · 2017: 1 · 2016: 1 · 2015: 1 · 2014: 1 · 2013: 2 · 2012: 5
FWCI
2.40
Type
journal article
Language
en
Open access
Licence
academic.oup.com/journals/pages/open_access/funder_policies/chorus/standard_publication_model (vor)
Locations
  • PLANT PHYSIOLOGY (publishedVersion)
  • PubMed Central (publishedVersion)
  • PubMed (publishedVersion)
Funders
  • Deutsche Forschungsgemeinschaft
  • National Institutes of Health (CRG 930555)
Topics
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Light effects on plants
  • Life Sciences › Agricultural and Biological Sciences › Plant Science › Plant Molecular Biology Research
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Photosynthetic Processes and Mechanisms
Keywords
phototropism, blue light, oat seedlings, Avena sativa, photoreceptors, protein phosphorylation, dark recovery
MeSH terms
Darkness, Dose-Response Relationship, Radiation, Light, Phosphorylation, Photic Stimulation, Plant Proteins, Time Factors, Phototropism, Cotyledon, Avena, Photosynthetic Reaction Center Complex Proteins

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