Structure and Expression of Chloroplast-Localized Porphobilinogen Deaminase from Pea (Pisum sativum L.) Isolated by Redundant Polymerase Chain Reaction

Witty, Michael; Wallace-Cook, Ashley D. M.; Albrecht, Huguette; Spano, Anthony; Michel, Hanspeter; Shabanowitz, Jefferey; Hunt, Donald F.; Timko, Michael P.; Smith, Alison G.

doi:10.1104/pp.103.1.139

Cited by 35 publications

(27 citation statements)

References 43 publications

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“…The detectable activity of ALA dehydratase and PBG deaminase in pea roots was found to be a maximum 5 d after germination and thereafter steadily declined (Smith, 1986). Additionally, maximum PBG deaminase activity was found in root tips compared with the older tissue in the elongation zone (Witty et al, 1993). Therefore, it is most likely that enzyme activity is present in roots but at levels too low to be assayed accurately.…”

Section: Discussionmentioning

confidence: 98%

“…As well as demonstrating the increase in plantspecific message levels, it also provided information about the spatial location of the transcripts within the nodule. The probes used were the cDNAs for soybean coprogen oxidase (Madsen et al, 1993), pea PBG deaminase (Witty et al, 1993), and pea ALA dehydratase (Boese et al, 1991). Antisense RNAs for each of these clones were prepared and hybridized to sections of soybean root nodules of 1 to 2 mm (3-4 weeks after infection), where the maximum induction of enzyme activity had been observed.…”

Section: In Situ Localization Of Transcripts For Heme Synthesis Enzymesmentioning

confidence: 99%

“…Sense and antisense RNA probes were prepared from the pea ALA dehydratase cDNA clone pALAD209 (Boese et al, 1991; a gift from Dr. M. Timko, University of Virginia, Charlottesville), the pea PBG deaminase cDNA clone pPD1 (Witty et al, 1993), and the soybean coprogen oxidase cDNA clone pCOF (Madsen et al, 1993). RNA was transcribed in vitro from each of these clones using SP6 or T7 polymerase, as appropriate, in the presence of 35 S-UTP (1250 Ci/mmol, Amersham) and was degraded to about 150-nucleotide-long fragments before hybridization.…”

Section: In Situ Hybridizationmentioning

confidence: 99%

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Evidence that the Plant Host Synthesizes the Heme Moiety of Leghemoglobin in Root Nodules1

et al. 1998

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Although it is well established that the plant host encodes and synthesizes the apoprotein for leghemoglobin in root nodules, the source of the heme moiety has been uncertain. We recently found that the transcript for coproporphyrinogen III oxidase, one of the later enzymes of heme synthesis, is highly elevated in soybean (Glycine max L.) nodules compared with roots. In this study we measured enzyme activity and carried out western-blot analysis and in situ hybridization of mRNA to investigate the levels during nodulation of the plant-specific coproporphyrinogen oxidase and four other enzymes of the pathway in both soybean and pea (Pisum sativum L.). We compared them with the activity found in leaves and uninfected roots. Our results demonstrate that all of these enzymes are elevated in the infected cells of nodules. Because these are the same cells that express apoleghemoglobin, the data strongly support a role for the plant in the synthesis of the heme moiety of leghemoglobin.

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Section: Discussionmentioning

confidence: 98%

Section: In Situ Localization Of Transcripts For Heme Synthesis Enzymesmentioning

confidence: 99%

Section: In Situ Hybridizationmentioning

confidence: 99%

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Evidence that the Plant Host Synthesizes the Heme Moiety of Leghemoglobin in Root Nodules1

et al. 1998

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“…In Chlamydomonas, the level of mRNA encoding PBGS increased about seven-fold upon transfer of synchronously growing cells from dark to light, with a corresponding three-fold increase in PBGS activity (Matters and Beale, 1995ab). By comparison, PBGS, PBGD, and UROS activities have been reported to increase three-to six-fold in etiolated pea leaves during the first 48-60 h of greening (Smith, 1986;Spano and Timko, 1991;Witty et al, 1993). In addition, expression of PBGS, PBGD, and CPOX appears to be regulated to a greater extent by developmental age rather than light, with higher levels of immunodetectable protein and mRNA found early in leaf development in the light or dark compared to later stages when the tissues are completely differentiated (He et al, 1994;Kruse et al, 1995).…”

Section: Light and Metabolic Regulation Of Chlorophyll Formationmentioning

confidence: 97%

“…However, up to this point only a very limited number of genes have been isolated from photosynthetic organisms (i.e., E. gracilis (Sharif et al, 1989), pea (Witty et al, 1993), and Arabidopsis (Lim et al, 1994)). When the deduced primary structure of the plant and algal PBGDs are compared to those from animals and bacteria, only 15-20% overall sequence similarity is observed (Shoolingin-Jordan, 1995).…”

Section: B Porphobilinogen Deaminasementioning

confidence: 99%

Pigment Biosynthesis: Chlorophylls, Heme, and Carotenoids

Timko

Advances in Photosynthesis and Respiration

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Proteomic analysis of de‐etiolated rice seedlings upon exposure to light

et al. 2007

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Two-week-old dark-grown rice seedlings were de-etiolated upon exposure to light. A comparison of 2-DE protein profiles between the dark-grown control and the rice seedlings illuminated respectively for 6, 12 and 24 h revealed 52 differentially expressed CBB-stained spots. Of these changed spots, the identity of 51 protein spots was determined by MALDI-TOF MS. Of these identified proteins, 13 proteins were related to light reactions of photosynthesis, photosynthetic carbon assimilation and chlorophyll biosynthesis, indicating the complex process of biogenesis of photosynthetic apparatus was correlated to the transition from a dark-grown (etiolated) to a light-grown (de-etiolated) morphology. In addition, three proteins related to antioxidation and detoxification decreased in de-etiolated rice seedlings implied, that the etiolated rice seedlings possibly be under an oxidative stress which could be released during their early stages of de-etiolation. The increase of S-adenosylmethionine synthetase that is involved in the biosynthesis of the phytohormone ethylene might contribute to the phenotypic development of the apical hook in the de-etiolated rice seedlings. These results yield a comprehensive picture of the post-transcriptional response for de-etiolation of rice seedlings and serve as a basic platform for further characterization of gene function and regulation in light-induced development of plants.

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Structure and Expression of Chloroplast-Localized Porphobilinogen Deaminase from Pea (Pisum sativum L.) Isolated by Redundant Polymerase Chain Reaction

Cited by 35 publications

References 43 publications

Evidence that the Plant Host Synthesizes the Heme Moiety of Leghemoglobin in Root Nodules1

Evidence that the Plant Host Synthesizes the Heme Moiety of Leghemoglobin in Root Nodules1

Pigment Biosynthesis: Chlorophylls, Heme, and Carotenoids

Proteomic analysis of de‐etiolated rice seedlings upon exposure to light

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