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Article ; Online: The Mechanisms of Molybdate Distribution and Homeostasis with Special Focus on the Model Plant

Weber, Jan-Niklas / Minner-Meinen, Rieke / Kaufholdt, David

2023 Volume 29, Issue 1

Abstract: This review article deals with the pathways of cellular and global molybdate distribution in plants, especially with a full overview for the model ... ...

Abstract	This review article deals with the pathways of cellular and global molybdate distribution in plants, especially with a full overview for the model plant
MeSH term(s)	Humans ; Molybdenum ; Arabidopsis ; Homeostasis ; Biological Transport
Chemical Substances	molybdate (14259-85-9) ; Molybdenum (81AH48963U)
Language	English
Publishing date	2023-12-20
Publishing country	Switzerland
Document type	Journal Article ; Review
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules29010040
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Article ; Online: Biosynthesis of polyprenylated xanthones in Hypericum perforatum roots involves 4-prenyltransferase.

Sayed, Hesham M B / Nassar, Sara / Kaufholdt, David / Beerhues, Ludger / Liu, Benye / El-Awaad, Islam

Plant physiology

2023 Volume 192, Issue 4, Page(s) 2971–2988

Abstract: Polyprenylated xanthones are natural products with a multitude of biological and pharmacological activities. However, their biosynthetic pathway is not completely understood. In this study, metabolic profiling revealed the presence of 4-prenylated 1,3,5, ... ...

Abstract	Polyprenylated xanthones are natural products with a multitude of biological and pharmacological activities. However, their biosynthetic pathway is not completely understood. In this study, metabolic profiling revealed the presence of 4-prenylated 1,3,5,6-tetrahydroxyxanthone derivatives in St. John's wort (Hypericum perforatum) root extracts. Transcriptomic data mining led to the detection of 5 variants of xanthone 4-prenyltransferase (HpPT4px) comprising 4 long variants (HpPT4px-v1 to HpPT4px-v4) and 1 short variant (HpPT4px-sh). The full-length sequences of all 5 variants were cloned and heterologously expressed in yeast (Saccharomyces cerevisiae). Microsomes containing HpPT4px-v2, HpPT4px-v4, and HpPT4px-sh catalyzed the addition of a prenyl group at the C-4 position of 1,3,5,6-tetrahydroxyxanthone; 1,3,5-trihydroxyxanthone; and 1,3,7-trihydroxyxanthone, whereas microsomes harboring HpPT4px-v1 and HpPT4px-v3 additionally accepted 1,3,6,7-tetrahydroxyxanthone. HpPT4px-v1 produced in Nicotiana benthamiana displayed the same activity as in yeast, while HpPT4px-sh was inactive. The kinetic parameters of HpPT4px-v1 and HpPT4px-sh chosen as representative variants indicated 1,3,5,6-tetrahydroxyxanthone as the preferred acceptor substrate, rationalizing that HpPT4px catalyzes the first prenylation step in the biosynthesis of polyprenylated xanthones in H. perforatum. Dimethylallyl pyrophosphate was the exclusive prenyl donor. Expression of the HpPT4px transcripts was highest in roots and leaves, raising the question of product translocation. C-terminal yellow fluorescent protein fusion of HpPT4px-v1 localized to the envelope of chloroplasts in N. benthamiana leaves, whereas short, truncated, and masked signal peptides led to the disruption of plastidial localization. These findings pave the way for a better understanding of the prenylation of xanthones in plants and the identification of additional xanthone-specific prenyltransferases.
MeSH term(s)	Hypericum/genetics ; Hypericum/metabolism ; Dimethylallyltranstransferase/genetics ; Dimethylallyltranstransferase/metabolism ; Saccharomyces cerevisiae/genetics ; Saccharomyces cerevisiae/metabolism ; Xanthones/metabolism ; Xanthones/pharmacology ; Plant Extracts/pharmacology
Chemical Substances	prenyl ; Dimethylallyltranstransferase (EC 2.5.1.1) ; Xanthones ; Plant Extracts
Language	English
Publishing date	2023-04-16
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	208914-2
ISSN	1532-2548 ; 0032-0889
ISSN (online)	1532-2548
ISSN	0032-0889
DOI	10.1093/plphys/kiad219
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Article: Cytosolic aromatic aldehyde dehydrogenase provides benzoic acid for xanthone biosynthesis in Hypericum

Singh, Poonam / Kaufholdt, David / Awadalah, Mina / Hänsch, Robert / Beerhues, Ludger / Gaid, Mariam

Plant physiology and biochemistry. 2021 Mar., v. 160

2021

Abstract: Benzoic acid is a building block of a multitude of well-known plant natural products, such as paclitaxel and cocaine. Its simple chemical structure contrasts with its complex biosynthesis. Hypericum species are rich in polyprenylated benzoic acid-derived ...

Abstract	Benzoic acid is a building block of a multitude of well-known plant natural products, such as paclitaxel and cocaine. Its simple chemical structure contrasts with its complex biosynthesis. Hypericum species are rich in polyprenylated benzoic acid-derived xanthones, which have received attention due to their biological impact on human health. The upstream biosynthetic sequence leading to xanthones is still incomplete. To supply benzoic acid for xanthone biosynthesis, Hypericum calycinum cell cultures use the CoA-dependent non-β-oxidative pathway, which starts with peroxisomal cinnamate CoA-ligase (HcCNL). Here, we use the xanthone-producing cell cultures to identify the transcript for benzaldehyde dehydrogenase (HcBD), a pivotal player in the non-β-oxidative pathways. In addition to benzaldehyde, the enzyme efficiently catalyzes the oxidation of trans-cinnamaldehyde in vitro. The enzymatic activity is strictly dependent on the presence of NAD⁺ as co-factor. HcBD is localized to the cytosol upon ectopic expression of reporter fusion constructs. HcBD oxidizes benzaldehyde, which moves across the peroxisome membrane, to form benzoic acid. Increases in the HcCNL and HcBD transcript levels precede the elicitor-induced xanthone accumulation. The current work addresses a crucial step in the yet incompletely understood CoA-dependent non-β-oxidative route of benzoic acid biosynthesis. Addressing this step may offer a new biotechnological tool to enhance product formation in biofactories.
Keywords	Hypericum calycinum ; aldehyde dehydrogenase ; benzaldehyde ; benzoic acid ; biosynthesis ; chemical structure ; cocaine ; cytosol ; enzyme activity ; human health ; oxidation ; paclitaxel ; plant physiology ; xanthone
Language	English
Dates of publication	2021-03
Size	p. 82-93.
Publishing place	Elsevier Masson SAS
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	742978-2
ISSN	1873-2690 ; 0981-9428
ISSN (online)	1873-2690
ISSN	0981-9428
DOI	10.1016/j.plaphy.2021.01.011
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Article ; Online: Cytosolic aromatic aldehyde dehydrogenase provides benzoic acid for xanthone biosynthesis in Hypericum.

Singh, Poonam / Kaufholdt, David / Awadalah, Mina / Hänsch, Robert / Beerhues, Ludger / Gaid, Mariam

Plant physiology and biochemistry : PPB

2021 Volume 160, Page(s) 82–93

Abstract	Benzoic acid is a building block of a multitude of well-known plant natural products, such as paclitaxel and cocaine. Its simple chemical structure contrasts with its complex biosynthesis. Hypericum species are rich in polyprenylated benzoic acid-derived xanthones, which have received attention due to their biological impact on human health. The upstream biosynthetic sequence leading to xanthones is still incomplete. To supply benzoic acid for xanthone biosynthesis, Hypericum calycinum cell cultures use the CoA-dependent non-β-oxidative pathway, which starts with peroxisomal cinnamate CoA-ligase (HcCNL). Here, we use the xanthone-producing cell cultures to identify the transcript for benzaldehyde dehydrogenase (HcBD), a pivotal player in the non-β-oxidative pathways. In addition to benzaldehyde, the enzyme efficiently catalyzes the oxidation of trans-cinnamaldehyde in vitro. The enzymatic activity is strictly dependent on the presence of NAD
MeSH term(s)	Aldehyde Oxidoreductases/metabolism ; Benzoic Acid/metabolism ; Hypericum/enzymology ; Plant Proteins/metabolism ; Xanthones/metabolism
Chemical Substances	Plant Proteins ; Xanthones ; Benzoic Acid (8SKN0B0MIM) ; Aldehyde Oxidoreductases (EC 1.2.-) ; benzaldehyde dehydrogenase (NAD+) (EC 1.2.1.28)
Language	English
Publishing date	2021-01-12
Publishing country	France
Document type	Journal Article
ZDB-ID	742978-2
ISSN	1873-2690 ; 0981-9428
ISSN (online)	1873-2690
ISSN	0981-9428
DOI	10.1016/j.plaphy.2021.01.011
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Article: Impact of wildfires on SO2 detoxification mechanisms in leaves of oak and beech trees

Weber, Jan-Niklas / Kaufholdt, David / Minner-Meinen, Rieke / Bloem, Elke / Shahid, Afsheen / Rennenberg, Heinz / Hänsch, Robert

Environmental pollution. 2021 Mar. 01, v. 272

2021

Abstract: Frequency and intensity of wildfire occurrences are dramatically increasing worldwide due to global climate change, having a devastating effect on the entire ecosystem including plants. Moreover, distribution of fire-smoke can influence the natural ... ...

Abstract	Frequency and intensity of wildfire occurrences are dramatically increasing worldwide due to global climate change, having a devastating effect on the entire ecosystem including plants. Moreover, distribution of fire-smoke can influence the natural environment over very long distances, i.e. hundreds of kilometres. Dry plant matter contains 0.1–0.9% (w/w) sulphur, which is mainly released during combustion into the atmosphere as sulphur dioxide (SO₂) resulting in local concentrations of up to 3000 nL L⁻¹. SO₂ is a highly hazardous gas, which enters plants mostly via the stomata. Toxic sulphite is formed inside the leaves due to conversion of SO₂. Plants as sessile organisms cannot escape from threats, why they evolved an impressive diversity of molecular defence mechanisms. In the present study, two recent wildfires in Germany were evaluated to analyse the effect of SO₂ released into the atmosphere on deciduous trees: the Meppen peat fire in 2018 and the forest fire close to Luebtheen in 2019. Collected leaf material from beech (Fagus sylvatica) and oak (Quercus robur) was examined with respect to detoxification of sulphur surplus due to the exposure to elevated SO₂. An induced stress reaction in both species was indicated by a 1.5-fold increase in oxidized glutathione. In beech leaves, the enzymatic activities of the sulphite detoxification enzymes sulphite oxidase and apoplastic peroxidases were increased 5-fold and a trend of sulphate accumulation was observed. In contrast, oaks did not regulate these enzymes during smoke exposure, however, the constitutive activity is 10-fold and 3-fold higher than in beech. These results show for the first time sulphite detoxification strategies of trees in situ after natural smoke exposure. Beech and oak trees survived short-term SO₂ fumigation due to exclusion of toxic gases and different oxidative detoxification strategies. Beeches use efficient upregulation of oxidative sulphite detoxification enzymes, while oaks hold a constitutively high enzyme-pool available.
Keywords	Fagus sylvatica ; Quercus robur ; climate change ; combustion ; ecosystems ; forest fires ; fumigation ; glutathione ; peat ; peroxidases ; pollution ; smoke ; sulfates ; sulfite oxidase ; sulfites ; sulfur ; sulfur dioxide ; toxicity ; Germany
Language	English
Dates of publication	2021-0301
Publishing place	Elsevier Ltd
Document type	Article
Note	NAL-AP-2-clean
ZDB-ID	280652-6
ISSN	1873-6424 ; 0013-9327 ; 0269-7491
ISSN (online)	1873-6424
ISSN	0013-9327 ; 0269-7491
DOI	10.1016/j.envpol.2020.116389
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Article ; Online: A promiscuous coenzyme A ligase provides benzoyl-coenzyme A for xanthone biosynthesis in Hypericum.

Singh, Poonam / Preu, Lutz / Beuerle, Till / Kaufholdt, David / Hänsch, Robert / Beerhues, Ludger / Gaid, Mariam

The Plant journal : for cell and molecular biology

2020 Volume 104, Issue 6, Page(s) 1472–1490

Abstract: Benzoic acid-derived compounds, such as polyprenylated benzophenones and xanthones, attract the interest of scientists due to challenging chemical structures and diverse biological activities. The genus Hypericum is of high medicinal value, as ... ...

Abstract	Benzoic acid-derived compounds, such as polyprenylated benzophenones and xanthones, attract the interest of scientists due to challenging chemical structures and diverse biological activities. The genus Hypericum is of high medicinal value, as exemplified by H. perforatum. It is rich in benzophenone and xanthone derivatives, the biosynthesis of which requires the catalytic activity of benzoate-coenzyme A (benzoate-CoA) ligase (BZL), which activates benzoic acid to benzoyl-CoA. Despite remarkable research so far done on benzoic acid biosynthesis in planta, all previous structural studies of BZL genes and proteins are exclusively related to benzoate-degrading microorganisms. Here, a transcript for a plant acyl-activating enzyme (AAE) was cloned from xanthone-producing Hypericum calycinum cell cultures using transcriptomic resources. An increase in the HcAAE1 transcript level preceded xanthone accumulation after elicitor treatment, as previously observed with other pathway-related genes. Subcellular localization of reporter fusions revealed the dual localization of HcAAE1 to cytosol and peroxisomes owing to a type 2 peroxisomal targeting signal. This result suggests the generation of benzoyl-CoA in Hypericum by the CoA-dependent non-β-oxidative route. A luciferase-based substrate specificity assay and the kinetic characterization indicated that HcAAE1 exhibits promiscuous substrate preference, with benzoic acid being the sole aromatic substrate accepted. Unlike 4-coumarate-CoA ligase and cinnamate-CoA ligase enzymes, HcAAE1 did not accept 4-coumaric and cinnamic acids, respectively. The substrate preference was corroborated by in silico modeling, which indicated valid docking of both benzoic acid and its adenosine monophosphate intermediate in the HcAAE1/BZL active site cavity.
MeSH term(s)	Acyl Coenzyme A/metabolism ; Cloning, Molecular ; Coenzyme A Ligases/genetics ; Coenzyme A Ligases/metabolism ; Cytosol/enzymology ; Hypericum/enzymology ; Hypericum/metabolism ; Metabolic Networks and Pathways ; Molecular Docking Simulation ; Peroxisomes/enzymology ; Phylogeny ; Plant Proteins/genetics ; Plant Proteins/metabolism ; Xanthones/metabolism
Chemical Substances	Acyl Coenzyme A ; Plant Proteins ; Xanthones ; benzoyl-coenzyme A (6756-74-7) ; xanthone (9749WEV0CA) ; Coenzyme A Ligases (EC 6.2.1.-)
Language	English
Publishing date	2020-11-03
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1088037-9
ISSN	1365-313X ; 0960-7412
ISSN (online)	1365-313X
ISSN	0960-7412
DOI	10.1111/tpj.15012
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Article ; Online: Moonlighting Arabidopsis molybdate transporter 2 family and GSH-complex formation facilitate molybdenum homeostasis.

Weber, Jan-Niklas / Minner-Meinen, Rieke / Behnecke, Maria / Biedendieck, Rebekka / Hänsch, Veit G / Hercher, Thomas W / Hertweck, Christian / van den Hout, Lena / Knüppel, Lars / Sivov, Simon / Schulze, Jutta / Mendel, Ralf-R / Hänsch, Robert / Kaufholdt, David

Communications biology

2023 Volume 6, Issue 1, Page(s) 801

Abstract: Molybdenum (Mo) as essential micronutrient for plants, acts as active component of molybdenum cofactor (Moco). Core metabolic processes like nitrate assimilation or abscisic-acid biosynthesis rely on Moco-dependent enzymes. Although a family of molybdate ...

Abstract	Molybdenum (Mo) as essential micronutrient for plants, acts as active component of molybdenum cofactor (Moco). Core metabolic processes like nitrate assimilation or abscisic-acid biosynthesis rely on Moco-dependent enzymes. Although a family of molybdate transport proteins (MOT1) is known to date in Arabidopsis, molybdate homeostasis remained unclear. Here we report a second family of molybdate transporters (MOT2) playing key roles in molybdate distribution and usage. KO phenotype-analyses, cellular and organ-specific localization, and connection to Moco-biosynthesis enzymes via protein-protein interaction suggest involvement in cellular import of molybdate in leaves and reproductive organs. Furthermore, we detected a glutathione-molybdate complex, which reveals how vacuolar storage is maintained. A putative Golgi S-adenosyl-methionine transport function was reported recently for the MOT2-family. Here, we propose a moonlighting function, since clear evidence of molybdate transport was found in a yeast-system. Our characterization of the MOT2-family and the detection of a glutathione-molybdate complex unveil the plant-wide way of molybdate.
MeSH term(s)	Arabidopsis/genetics ; Arabidopsis/metabolism ; Molybdenum/metabolism ; Membrane Transport Proteins/genetics ; Membrane Transport Proteins/metabolism ; Pteridines ; Homeostasis
Chemical Substances	molybdate (14259-85-9) ; Molybdenum (81AH48963U) ; Membrane Transport Proteins ; Pteridines
Language	English
Publishing date	2023-08-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ISSN	2399-3642
ISSN (online)	2399-3642
DOI	10.1038/s42003-023-05161-x
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Article ; Online: Physiological Importance of Molybdate Transporter Family 1 in Feeding the Molybdenum Cofactor Biosynthesis Pathway in

Minner-Meinen, Rieke / Weber, Jan-Niklas / Kistner, Sarah / Meyfarth, Paul / Saudhof, Merve / van den Hout, Lena / Schulze, Jutta / Mendel, Ralf-Rainer / Hänsch, Robert / Kaufholdt, David

Molecules (Basel, Switzerland)

2022 Volume 27, Issue 10

Abstract: Molybdate uptake and molybdenum cofactor (Moco) biosynthesis were investigated in detail in the last few decades. The present study critically reviews our present knowledge about eukaryotic molybdate transporters (MOT) and focuses on the model ... ...

Abstract	Molybdate uptake and molybdenum cofactor (Moco) biosynthesis were investigated in detail in the last few decades. The present study critically reviews our present knowledge about eukaryotic molybdate transporters (MOT) and focuses on the model plant
MeSH term(s)	Anion Transport Proteins/metabolism ; Arabidopsis/genetics ; Arabidopsis/metabolism ; Molybdenum/metabolism ; Molybdenum Cofactors
Chemical Substances	Anion Transport Proteins ; Molybdenum Cofactors ; molybdate (14259-85-9) ; Molybdenum (81AH48963U)
Language	English
Publishing date	2022-05-15
Publishing country	Switzerland
Document type	Journal Article
ZDB-ID	1413402-0
ISSN	1420-3049 ; 1431-5165 ; 1420-3049
ISSN (online)	1420-3049
ISSN	1431-5165 ; 1420-3049
DOI	10.3390/molecules27103158
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Article ; Online: Impact of wildfires on SO

Weber, Jan-Niklas / Kaufholdt, David / Minner-Meinen, Rieke / Bloem, Elke / Shahid, Afsheen / Rennenberg, Heinz / Hänsch, Robert

Environmental pollution (Barking, Essex : 1987)

2020 Volume 272, Page(s) 116389

Abstract	Frequency and intensity of wildfire occurrences are dramatically increasing worldwide due to global climate change, having a devastating effect on the entire ecosystem including plants. Moreover, distribution of fire-smoke can influence the natural environment over very long distances, i.e. hundreds of kilometres. Dry plant matter contains 0.1-0.9% (w/w) sulphur, which is mainly released during combustion into the atmosphere as sulphur dioxide (SO
MeSH term(s)	Ecosystem ; Fagus ; Germany ; Plant Leaves ; Quercus ; Trees ; Wildfires
Language	English
Publishing date	2020-12-30
Publishing country	England
Document type	Journal Article
ZDB-ID	280652-6
ISSN	1873-6424 ; 0013-9327 ; 0269-7491
ISSN (online)	1873-6424
ISSN	0013-9327 ; 0269-7491
DOI	10.1016/j.envpol.2020.116389
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Article: Split-HaloTag imaging assay for sophisticated microscopy of protein–protein interactions in planta

Minner-Meinen, Rieke / Weber, Jan-Niklas / Albrecht, Andreas / Matis, Rainer / Behnecke, Maria / Tietge, Cindy / Frank, Stefan / Schulze, Jutta / Buschmann, Henrik / Walla, Peter Jomo / Mendel, Ralf-R / Hänsch, Robert / Kaufholdt, David

Plant communications. 2021 June 10,

2021

Abstract: An ever-increasing number of intracellular multi-protein networks have been identified in plant cells. Split-GFP-based protein–protein interaction assays combine the advantages of in vivo interaction studies in a native environment with additional ... ...

Abstract	An ever-increasing number of intracellular multi-protein networks have been identified in plant cells. Split-GFP-based protein–protein interaction assays combine the advantages of in vivo interaction studies in a native environment with additional visualization of protein complex localization. Because of their simple protocols, they have become some of the most frequently used methods. However, standard fluorescent proteins present several drawbacks for sophisticated microscopy. With the HaloTag system, these drawbacks can be overcome, as this reporter forms covalent irreversible bonds with synthetic photostable fluorescent ligands. Dyes can be used in adjustable concentrations and are suitable for advanced microscopy methods. Therefore, we have established the Split-HaloTag imaging assay in plants, which is based on the reconstitution of a functional HaloTag protein upon protein–protein interaction and the subsequent covalent binding of an added fluorescent ligand. Its suitability and robustness were demonstrated using a well-characterized interaction as an example of protein–protein interaction at cellular structures: the anchoring of the molybdenum cofactor biosynthesis complex to filamentous actin. In addition, a specific interaction was visualized in a more distinctive manner with subdiffractional polarization microscopy, Airyscan, and structured illumination microscopy to provide examples of sophisticated imaging. Split-GFP and Split-HaloTag can complement one another, as Split-HaloTag represents an alternative option and an addition to the large toolbox of in vivo methods. Therefore, this promising new Split-HaloTag imaging assay provides a unique and sensitive approach for more detailed characterization of protein–protein interactions using specific microscopy techniques, such as 3D imaging, single-molecule tracking, and super-resolution microscopy.
Keywords	actin ; biosynthesis ; fluorescence ; ligands ; lighting ; molybdenum ; polarized light microscopy ; protein-protein interactions
Language	English
Dates of publication	2021-0610
Publishing place	Elsevier Inc.
Document type	Article
Note	Pre-press version
ISSN	2590-3462
DOI	10.1016/j.xplc.2021.100212
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