In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli

Edgerton, Michael D.; Santos, Michael O.; Jones, Alan M.

doi:10.1007/bf00023616

Cited by 10 publications

(5 citation statements)

References 22 publications

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“…Higher plant phytochrome is an ellipsoidal dimer in its native state: the subdomain responsible for cohesion (33) is in the region missing from Synechocystis phytochrome. Indeed, size exclusion chromatography data (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…Furthermore, similar SAR values were obtained for preparations from clones coexpressing GroES and GroEL chaperonins. Such coexpression often has dramatic effects on the solubility, quarternary assembly and activity of recombinant proteins, including phytochromes, in E. coli (8,33,40). If the low SAR resulted from a proportion of the apoprotein that was unable to autoassemble or become spectrally active, differences would probably have emerged; we are, however, currently unable to exclude the possibility.…”

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confidence: 98%

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Characterization of recombinant phytochrome from the cyanobacterium Synechocystis

Lamparter

Mittmann

Gärtner

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

173

223

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following correction should be noted. Due to an editorial change at PNAS, the meaning of the last sentence on page 14046 was altered. The sentence originally read as follows: On the other hand, this structure does not reproduce the pharmacological properties of either P or Q channel exactly, as the ID 50 to sFTX and -Aga IVA for P-type channels is lower than for the ␣1A, ␣2␦, ␤Ib channels in HEK cells.Neurobiology. In the article "The synthesis of ATP by glycolytic enzymes in the postsynaptic density and the effect of endogenously generated nitric oxide" Kuo Wu, Chiye Aoki, Alice Elste, Adrienne A. Rogalski-Wilk, and Philip Siekevitz, which appeared in number 24, November 25, 1997, of Proc. Natl. Acad. Sci. USA (94,(13273)(13274)(13275)(13276)(13277)(13278), the quality of the reproduction of Fig. 2A was poor. The figure and its legend are shown below:Biochemistry. In the article "KSR stimulates Raf-1 activity in a kinase-independent manner" by Neil R. Michaud, Marc Therrien, Angela Cacace, Lisa C. Edsall, Sarah Spiegel, Gerald M. Rubin, and Deborah K. Morrison, which appeared in number 24, November 25, 1997, of Proc. Natl. Acad. Sci. USA (94,(12792)(12793)(12794)(12795)(12796), the following correction should be noted.Due to a printer's error, background was incorrectly added to (50 g) and 100 g each of the other fractions, in 100 l final volume, including whole homogenate (H), synaptosomes (Syn), synaptic plasma membranes (SPM), and crude synaptic vesicles (CSV), were incubated at 37°C for 15 min. NAD incorporation was performed in the absence (Ϫ) or presence (ϩ) of SNP as exogenous source of NO. The mixtures were subjected to SDS͞PAGE and then autoradiography. (B) Western blot analysis of the G3PD in the subcellular fractions. To confirm that the radioactive protein in the subcellular fractions was indeed G3PD, Western blot analysis was performed by using specific anti-G3PD antibodies as described.

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Section: Discussionmentioning

confidence: 99%

mentioning

confidence: 98%

Characterization of recombinant phytochrome from the cyanobacterium Synechocystis

Lamparter

Mittmann

Gärtner

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

173

223

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“…However, this approach has been hampered by the lack of a relevant in vitro assay of Pfr activity (Quail, 1991) and by the complicated assembly of the chromoprotein that is difficult to reproduce with high yields in vitro or in microorganisms (Wahleithner et al, 1991;Edgerton et al, 1993;Furuya and Song, 1994). To overcome these limitations, one strategy now used is to ectopically express phytochrome genes in transgenic plants (for review, see Cherry and Vierstra, 1994).…”

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confidence: 99%

Phytochrome A Overexpression in Transgenic Tobacco (Correlation of Dwarf Phenotype with High Concentrations of Phytochrome in Vascular Tissue and Attenuated Gibberellin Levels)

Jordan

Hatfield²,

Hondred³

et al. 1995

Plant Physiol.

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Phytochromes are a family of related chromoproteins that regulate photomorphogenesis in plants. Ectopic overexpression of the phytochrome A in severa1 plant species has pleiotropic effects, including substantial dwarfing, increased pigmentation, and delayed leaf senescence. We show here that the dwarf response is related to a reduction in active gibberellins (CAs) in tobacco (Nicofiana fabacum) overexpressing oat phytochrome A under the control of the cauliflower mosaic virus (CaMV) 35s promoter and can be suppressed by foliar applications of gibberellic acid. In transgenic seedlings, high concentrations of oat phytochrome A were detected in stem and petiole vascular tissue (consistent with the activity of the CaMV 35s promoter), implicating vascular tissue as a potential site of phytochrome A action. To examine the efficacy of this cellular site, oat phytochrome A was also expressed using Arabidopsis chlorophyll a/b-binding protein (CAB) and the Arabidopsis ubiquitin (UBQ7) promoters. Neither promoter was as effective as CaMV 35s in expressing phytochrome in vascular tissue or in inducing the dwarf phenotype. Collectively, these data indicate that the spatial distribution of ectopic phytochrome i s important in eliciting the dwarf response and suggest that the phenotype is invoked by elevated levels of the far-red-absorbing form of phytochrome within vascular tissue repressing CA biosynthesis.Phytochromes are a family of regulatory photoreceptors in plants that measure both the quantity and quality of available light (for reviews, see Quail, 1991;Vierstra, 1993;Kendrick and Kronenberg, 1994). They are dimeric, cytoplasmic proteins, with each subunit consisting of a linear tetrapyrrole chromophore covalently linked to an approx-

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“…Recently, we (Edgerton et al, 1993) and others Mummert et al, 1993) demonstrated the involvement of the chaperonins GroEL/S in phytochrome folding. This aggregation is probably due to limiting amounts of a chaperone present in the wheat germ translation system.…”

Section: Resultsmentioning

confidence: 93%

Subunit interactions in the carboxy-terminal domain of phytochrome

Edgerton¹,

Jones²

1993

Biochemistry

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We have produced defined fragments of the oat PhyA AP3 protein using an in vitro translation system and analyzed the quaternary structure of these fragments by size exclusion chromatography. Sequences between amino acids S599 and L683 are shown to dimerize by this in vitro assay and by a lambda repressor-based in vivo assay. A subset of this dimerization region, V623-S673, which has previously been identified as being involved in interdomain interactions on the basis of the behavior of overlapping constructs in a lambda repressor assay for protein-protein interaction, is shown by both assays to be necessary but insufficient for dimerization. Sequences between L685 and R815, which are unable to dimerize by themselves, are shown to interact with sequences between S599 and L683. Sequences E1069-Q1129, also previously suggested to be involved in dimerization, are shown here not to be required for phytochrome dimerization. These results based on an in vitro assay have confirmed some of the results previously obtained using an in vivo assay and extend these earlier results by revealing new protein-protein interactions. This dissection of sequences involved in phytochrome dimerization taken together with previous work has enabled us to propose a model for the behavior of the dimerization region where the core structure involved in dimerization is located on both sides of a region around residue 750 found at the surface.

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In vivo suppression of phytochrome aggregation by the GroE chaperonins in Escherichia coli

Cited by 10 publications

References 22 publications

Characterization of recombinant phytochrome from the cyanobacterium Synechocystis

Characterization of recombinant phytochrome from the cyanobacterium Synechocystis

Phytochrome A Overexpression in Transgenic Tobacco (Correlation of Dwarf Phenotype with High Concentrations of Phytochrome in Vascular Tissue and Attenuated Gibberellin Levels)

Subunit interactions in the carboxy-terminal domain of phytochrome

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