Plant tissue culture media

Gamborg, O. L.; Murashige, Toshio; Thorpe, Trevor A.; Vasil, Indra K.

doi:10.1007/bf02796489

Cited by 337 publications

(142 citation statements)

References 18 publications

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“…petite Havana were germinated on B5-modified medium (18), and leaves of 3-4-week-old plants were used in all experiments. Protoplast isolation and transient transformation were performed as described previously (19).…”

Section: Methodsmentioning

confidence: 99%

Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Aseeva

Ossenbühl

Eichacker

et al. 2004

Journal of Biological Chemistry

117

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Vipp1 (vesicle-inducing protein in plastids 1) is found in Cyanobacteria and chloroplasts of photosynthetic eukaryotes where it is essential for the formation of the thylakoid membrane. Vipp1 is closely related to the phage shock protein A (PspA), a bacterial protein induced under diverse stress conditions. Vipp1 proteins differ from PspA by an additional C-terminal domain that is required for Vipp1 function in thylakoid biogenesis. We show here that in Cyanobacteria, green algae, and vascular plants, Vipp1 is part of a high molecular mass complex. The complex is formed by multiple copies of Vipp1, and complex formation involves interaction of the central ␣-helical domain that is common to Vipp1 as well as to PspA proteins. In chloroplasts of vascular plants, the Vipp1 complex can be visualized by green fluorescent protein fusion in discrete locations at the inner envelope. Green fluorescent protein fusion analysis furthermore revealed that complex formation is important for proper positioning of Vipp1 at the inner envelope of chloroplasts.Oxygenic photosynthesis is a specific feature of Cyanobacteria and chloroplasts of plants and algae. Characteristic of oxygenic photosynthesis is a specialized membrane system, the thylakoids, on which the components of the photosynthetic machinery are located (1). Despite its importance in the process of oxygenic photosynthesis, very little is known about the origin of the thylakoid membrane system in the ancestry of present day Cyanobacteria. Furthermore, proteins and other factors that are involved in the formation and maintenance of the thylakoid membrane in either Cyanobacteria or chloroplasts are not well defined.We have shown recently that in Arabidopsis as well as in Synechocystis the Vipp1 1 protein is essential for thylakoid biogenesis (2, 3). ⌬-vipp1 mutants, in which the expression of the vipp1 gene is greatly reduced, have lost their ability to build up a thylakoid membrane system and to perform oxygenic photosynthesis (2, 3). Interestingly, disruption of the vipp1 gene in Arabidopsis also abolished chloroplast vesicle transport, which has an alleged function in thylakoid formation in the chloroplasts of higher plants (2, 4). Vipp1 is closely related to PspA, a bacterial protein that is induced under distinct stress conditions, i.e. invasion by filamentous phages, inhibition of lipid biosynthesis, secretion defects, or the saturation of the twin arginine pathway (5-8). PspA and Vipp1 are distinguished by a C-terminal domain of about 20 -30 amino acids which is present in all Vipp1 proteins but lacking in PspA (3). It is presumed that this C-terminal extension is important for the role of Vipp1 in thylakoid biogenesis. Most Cyanobacteria possess genes coding for both PspA and Vipp1. Chloroplasts seem to have retained solely Vipp1, indicating that the function of PspA is no longer required in this organelle.So far, the exact function of PspA and Vipp1 remains elusive. In bacteria, PspA is part of a larger operon encoding four more proteins, PspB-PspE. PspA is induce...

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Section: Methodsmentioning

confidence: 99%

Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Aseeva

Ossenbühl

Eichacker

et al. 2004

Journal of Biological Chemistry

117

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“…Due to inconsistencies in the literature, the salt formulations of some media were corrected as follows: Murashige & Skoog (1962) ZnSO^HjO corrected from ZnS04'4H20, 37.2 mg I" 1 Na2-EDTA'2H20 (see Singh & Krikorian 1980);White (1963) NajSO, corrected from NaS04, 19 mg I' 1 NaH2P04 H20, ferric sulfate replaced with equivalent amount of ferrous sulfate in chelated form (see Singh & Krikorian, 1981); B5 (Gamborg et al 1968) iron replaced with MS iron formulation and CuS04'5H20 corrected from CuS04 (see Gamborg et al 1976); Nitsch & Nitsch (1969) 5.57g FeS04'7H20 in stock solution corrected from 0.557 g (see Nitsch 1977); Woody Plant Medium (Lloyd &McCown 1980) MnS04'4H20 corrected from MnS04'H20 (see Smith & McCown 1982/83). Schenk & Hildebrand!…”

Section: Methodsmentioning

confidence: 99%

Culture medium pH is influenced by basal medium, carbohydrate source, gelling agent, activated charcoal, and medium storage method

1991

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“…Subsequently, for 8 weeks, plants were watered twice a week. Once a week between the watering, we applied 8 ml of Hoagland solution modified after Gamborg and Wetter (1975) Table T1), after draining of excess irrigation water.…”

Section: Plant Material Growth Conditions and Amf Inoculationmentioning

confidence: 99%

Identification of arbuscular mycorrhiza-inducible Nitrate Transporter 1/Peptide Transporter Family (NPF) genes in rice

Drechsler¹,

Courty²,

Brulé³

et al. 2017

Mycorrhiza

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Arbuscular mycorrhizal fungi (AMF) colonize up to 90% of all land plants and facilitate the acquisition of mineral nutrients by their hosts. Inorganic orthophosphate (P i ) and nitrogen (N) are the major nutrients transferred from the fungi to plants. While plant P i transporters involved in nutrient transfer at the plant-fungal interface have been well studied, the plant N transporters participating in this process are largely unknown except for some ammonium transporters (AMT) specifically assigned to arbuscule-colonized cortical cells. In plants, many nitrate transporter 1/peptide transporter family (NPF) members are involved in the translocation of nitrogenous compounds including nitrate, amino acids, peptides and plant hormones. Whether NPF members respond to AMF colonization, however, is not yet known. Here, we investigated the transcriptional regulation of 82 rice (Oryza sativa) NPF genes in response to colonization by the AMF Rhizophagus irregularis in roots of plants grown under five different nutrition regimes. Expression of the four OsNPF genes NPF2.2/ PTR2, NPF1.3, NPF6.4 and NPF4.12 was strongly induced in mycorrhizal roots and depended on the composition of the fertilizer solution, nominating them as interesting candidates for nutrient signaling and exchange processes at the plantfungal interface.

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Plant tissue culture media

Cited by 337 publications

References 18 publications

Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Complex Formation of Vipp1 Depends on Its α-Helical PspA-like Domain

Culture medium pH is influenced by basal medium, carbohydrate source, gelling agent, activated charcoal, and medium storage method

Identification of arbuscular mycorrhiza-inducible Nitrate Transporter 1/Peptide Transporter Family (NPF) genes in rice

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