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Article ; Online: Ger1 is a secreted aspartic acid protease essential for spore germination in Ustilago maydis.

Mukherjee, Subhasish / Bhakta, Koustav / Ghosh, Abhrajyoti / Ghosh, Anupama

2023 Volume 40, Issue 2, Page(s) 102–116

Abstract: Ustilago maydis expresses a number of proteases during its pathogenic lifecycle. Some of the proteases including both intracellular and extracellular ones have previously been shown to influence the virulence of the pathogen. However, any role of ... ...

Abstract	Ustilago maydis expresses a number of proteases during its pathogenic lifecycle. Some of the proteases including both intracellular and extracellular ones have previously been shown to influence the virulence of the pathogen. However, any role of secreted proteases in the sporulation process of U. maydis have not been explored earlier. In this study we have investigated the biological function of one such secreted protease, Ger1 belonging to aspartic protease A1 family. An assessment of the real time expression of ger1 revealed an infection specific expression of the protein especially during late phases of infection. We also evaluated any contribution of the protein in the pathogenicity of the fungus. Our data revealed an involvement of Ger1 in the sporulation and spore germination processes of U. maydis. Ger1 also showed positive influence on the pathogenicity of the fungus and accordingly the ger1 deletion mutant exhibited reduced pathogenicity. The study also demonstrated the protease activity associated with Ger1 to be essential for its biological function. Fluorescence microscopy of maize plants infected with U. maydis cells expressing Ger1-mcherry-HA also revealed that Ger1 is efficiently secreted within maize apoplast.
MeSH term(s)	Aspartic Acid Proteases/genetics ; Aspartic Acid Proteases/metabolism ; Ustilago/genetics ; Ustilago/metabolism ; Basidiomycota ; Fungal Proteins/genetics ; Fungal Proteins/metabolism ; Spores/metabolism
Chemical Substances	Aspartic Acid Proteases (EC 3.4.-) ; Fungal Proteins
Language	English
Publishing date	2023-01-02
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	632636-5
ISSN	1097-0061 ; 0749-503X
ISSN (online)	1097-0061
ISSN	0749-503X
DOI	10.1002/yea.3835
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Article ; Online: Ger1 is a secreted aspartic acid protease essential for spore germination in Ustilago maydis

Mukherjee, Subhasish / Bhakta, Koustav / Ghosh, Abhrajyoti / Ghosh, Anupama

Yeast. 2023 Feb., v. 40, no. 2 p.102-116

2023

Abstract	Ustilago maydis expresses a number of proteases during its pathogenic lifecycle. Some of the proteases including both intracellular and extracellular ones have previously been shown to influence the virulence of the pathogen. However, any role of secreted proteases in the sporulation process of U. maydis have not been explored earlier. In this study we have investigated the biological function of one such secreted protease, Ger1 belonging to aspartic protease A1 family. An assessment of the real time expression of ger1 revealed an infection specific expression of the protein especially during late phases of infection. We also evaluated any contribution of the protein in the pathogenicity of the fungus. Our data revealed an involvement of Ger1 in the sporulation and spore germination processes of U. maydis. Ger1 also showed positive influence on the pathogenicity of the fungus and accordingly the ger1 deletion mutant exhibited reduced pathogenicity. The study also demonstrated the protease activity associated with Ger1 to be essential for its biological function. Fluorescence microscopy of maize plants infected with U. maydis cells expressing Ger1‐mcherry‐HA also revealed that Ger1 is efficiently secreted within maize apoplast.
Keywords	Ustilago zeae ; apoplast ; aspartic proteinases ; corn ; enzyme activity ; fluorescence microscopy ; mutants ; pathogens ; spore germination ; sporulation ; virulence ; yeasts
Language	English
Dates of publication	2023-02
Size	p. 102-116.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	632636-5
ISSN	1097-0061 ; 0749-503X
ISSN (online)	1097-0061
ISSN	0749-503X
DOI	10.1002/yea.3835
Database	NAL-Catalogue (AGRICOLA)

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Article: Defense Surveillance System at the Interface: Response of Rice Towards

Acharya, Udita / Das, Troyee / Ghosh, Zhumur / Ghosh, Anupama

Molecular plant-microbe interactions : MPMI

2022 , Page(s) MPMI07220153R

Abstract: Sheath blight of rice caused by necrotrophic plant ... ...

Abstract	Sheath blight of rice caused by necrotrophic plant pathogen
Language	English
Publishing date	2022-12-12
Publishing country	United States
Document type	Journal Article
ZDB-ID	743331-1
ISSN	1943-7706 ; 0894-0282
ISSN (online)	1943-7706
ISSN	0894-0282
DOI	10.1094/MPMI-07-22-0153-R
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Article ; Online: Small heat shock proteins (HSP12, HSP20 and HSP30) play a role in Ustilago maydis pathogenesis.

Ghosh, Anupama

FEMS microbiology letters

2014 Volume 361, Issue 1, Page(s) 17–24

Abstract: Small heat shock proteins (HSP) have multiple functions within a cell. These functions primarily include regulation of growth and survival in response to different stresses. However in some cases small HSPs have been shown to play crucial roles in ... ...

Abstract	Small heat shock proteins (HSP) have multiple functions within a cell. These functions primarily include regulation of growth and survival in response to different stresses. However in some cases small HSPs have been shown to play crucial roles in microbial pathogenesis. Ustilago maydis genome also codes for a number of small HSPs. In the present study we elucidate the role of U. maydis small HSPs in the pathogenicity as well as general stress response of the fungus. Through quantitative real time PCR analysis the expression levels of small HSP genes in comparison with other HSPs were assessed both during infection of the host plant Zea mays and when the pathogen was subjected to an abiotic stress such as oxidative stress. This study revealed that contrary to other HSPs, small HSPs showed an increased level of differential expression under both the tested conditions, indicating a possible role of small HSPs in the pathogenicity and stress response of U. maydis This has been further confirmed by generation of deletion and complementation strains of three putative small HSPs.
Language	English
Publishing date	2014-12
Publishing country	England
Document type	Journal Article
ZDB-ID	752343-9
ISSN	1574-6968 ; 0378-1097
ISSN (online)	1574-6968
ISSN	0378-1097
DOI	10.1111/1574-6968.12605
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Article ; Online: Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis

Mitra, Aroni / Bhakta, Koustav / Kar, Ankita / Roy, Anisha / Mohid, Sk Abdul / Ghosh, Abhrajyoti / Ghosh, Anupama

Molecular Plant Pathology. 2023 Sept., v. 24, no. 9 p.1063-1077

2023

Abstract: Small heat shock proteins (sHsps) play diverse roles in the stress response and maintenance of cellular functions. The Ustilago maydis genome codes for few sHsps. Among these, Hsp12 has previously been demonstrated to be involved in the pathogenesis of ... ...

Abstract	Small heat shock proteins (sHsps) play diverse roles in the stress response and maintenance of cellular functions. The Ustilago maydis genome codes for few sHsps. Among these, Hsp12 has previously been demonstrated to be involved in the pathogenesis of the fungus by our group. In the present study we further investigated the biological function of the protein in the pathogenic development of U. maydis. Analysis of the primary amino acid sequence of Hsp12 in combination with spectroscopic methods to analyse secondary protein structures revealed an intrinsically disordered nature of the protein. We also carried out detailed analysis on the protein aggregation prevention activity associated with Hsp12. Our data suggest Hsp12 has trehalose‐dependent protein aggregation prevention activity. Through assaying the interaction of Hsp12 with lipid membranes in vitro we also showed the ability of U. maydis Hsp12 to induce stability in lipid vesicles. U. maydis hsp12 deletion mutants exhibited defects in the endocytosis process and delayed completion of the pathogenic life cycle. Therefore, U. maydis Hsp12 contributes to the pathogenic development of the fungus through its ability to relieve proteotoxic stress during infection as well as its membrane‐stabilizing function.
Keywords	Ustilago zeae ; amino acid sequences ; endocytosis ; fungi ; genome ; heat shock proteins ; heat stress ; lipids ; pathogenesis ; plant pathology ; spectroscopy ; stress response
Language	English
Dates of publication	2023-09
Size	p. 1063-1077.
Publishing place	John Wiley & Sons, Ltd
Document type	Article ; Online
Note	JOURNAL ARTICLE
ZDB-ID	2020755-4
ISSN	1364-3703 ; 1464-6722
ISSN (online)	1364-3703
ISSN	1464-6722
DOI	10.1111/mpp.13350
Database	NAL-Catalogue (AGRICOLA)

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Article: Archaeal Hsp14 drives substrate shuttling between small heat shock proteins and thermosome: insights into a novel substrate transfer pathway

Roy, Mousam / Bhakta, Koustav / Bhowmick, Arghya / Gupta, Sayandeep / Ghosh, Anupama / Ghosh, Abhrajyoti

FEBS journal. 2022 Feb., v. 289, no. 4

2022

Abstract: Heat shock proteins maintain protein homeostasis and facilitate the survival of an organism under stress. Archaeal heat shock machinery usually consists of only sHsps, Hsp70, and Hsp60. Moreover, Hsp70 is absent in thermophilic and hyperthermophilic ... ...

Abstract	Heat shock proteins maintain protein homeostasis and facilitate the survival of an organism under stress. Archaeal heat shock machinery usually consists of only sHsps, Hsp70, and Hsp60. Moreover, Hsp70 is absent in thermophilic and hyperthermophilic archaea. In the absence of Hsp70, how aggregating protein substrates are transferred to Hsp60 for refolding remains elusive. Here, we investigated the crosstalk in the heat shock response pathway of thermoacidophilic crenarchaeon Sulfolobus acidocaldarius. In the present study, we biophysically and biochemically characterized one of the small heat shock proteins, Hsp14, of S. acidocaldarius. Moreover, we investigated its ability to interact with Hsp20 and Hsp60 to facilitate the substrate proteins' folding under stress conditions. Like Hsp20, we demonstrated that the dimer is the active form of Hsp14, and it forms an oligomeric storage form at a higher temperature. More importantly, the dynamics of the Hsp14 oligomer are maintained by rapid subunit exchange between the dimeric states, and the rate of subunit exchange increases with increasing temperature. We also tested the ability of Hsp14 to form hetero‐oligomers via subunit exchange with Hsp20. We observed hetero‐oligomer formation only at higher temperatures (50 °C–70 °C). Furthermore, experiments were performed to investigate the interaction between small heat shock proteins and Hsp60. We demonstrated an enthalpy‐driven direct physical interaction between Hsp14 and Hsp60. Our results revealed that Hsp14 could transfer sHsp‐captured substrate proteins to Hsp60, which then refolds them back to their active form.
Keywords	Sulfolobus ; heat shock response ; heat stress ; homeostasis ; hyperthermophilic archaea ; temperature
Language	English
Dates of publication	2022-02
Size	p. 1080-1104.
Publishing place	John Wiley & Sons, Ltd
Document type	Article
Note	JOURNAL ARTICLE
ZDB-ID	2173655-8
ISSN	1742-4658 ; 1742-464X
ISSN (online)	1742-4658
ISSN	1742-464X
DOI	10.1111/febs.16226
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Article ; Online: Ustilago maydis secreted T2 ribonucleases, Nuc1 and Nuc2 scavenge extracellular RNA.

Mukherjee, Dibya / Gupta, Sayandeep / Ghosh, Abhrajyoti / Ghosh, Anupama

Cellular microbiology

2020 Volume 22, Issue 12, Page(s) e13256

Abstract: Ustilago maydis genome codes for many secreted ribonucleases. The contribution of two among these belonging to the T2 family (Nuc1 and Nuc2) in the pathogen virulence, has been assessed in this study. The nuc1 and nuc2 deletion mutants showed not only ... ...

Abstract	Ustilago maydis genome codes for many secreted ribonucleases. The contribution of two among these belonging to the T2 family (Nuc1 and Nuc2) in the pathogen virulence, has been assessed in this study. The nuc1 and nuc2 deletion mutants showed not only reduced pathogenicity compared to the SG200 WT strain but also exhibited significant delay in the completion of the pathogenic lifecycle. Both the proteins were also tested for their nucleolytic activities towards RNA substrates from maize and yeast. This also yielded valuable insights into the ability of the ribonucleases to utilise extracellular RNA as a nutrient source. Our study therefore established a role of two T2 type secreted ribonucleases of a phytopathogen in the acquisition of nutrient for the first time. This study also provides evidence that maize apoplast contains RNA, which can be utilised as a substrate by both Nuc1 and Nuc2.
MeSH term(s)	Antigens, Fungal ; Basidiomycota/enzymology ; Basidiomycota/genetics ; Basidiomycota/metabolism ; Basidiomycota/pathogenicity ; Endoribonucleases/classification ; Endoribonucleases/genetics ; Endoribonucleases/metabolism ; Fungal Proteins/metabolism ; Gene Deletion ; Gene Expression Regulation, Fungal ; Host-Pathogen Interactions ; RNA/metabolism ; Virulence/genetics ; Virulence Factors/genetics ; Virulence Factors/metabolism ; Zea mays/metabolism
Chemical Substances	Antigens, Fungal ; Fungal Proteins ; Virulence Factors ; RNA (63231-63-0) ; Endoribonucleases (EC 3.1.-) ; ribonuclease T(2) (EC 3.1.27.1)
Language	English
Publishing date	2020-09-14
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	1468320-9
ISSN	1462-5822 ; 1462-5814
ISSN (online)	1462-5822
ISSN	1462-5814
DOI	10.1111/cmi.13256
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Article: Small heat shock proteins (HSP12, HSP20 and HSP30) play a role in Ustilago maydis pathogenesis

Ghosh, Anupama

FEMS microbiology letters. 2014 Dec., v. 361, no. 1

2014

Abstract	Small heat shock proteins (HSP) have multiple functions within a cell. These functions primarily include regulation of growth and survival in response to different stresses. However in some cases small HSPs have been shown to play crucial roles in microbial pathogenesis. Ustilago maydis genome also codes for a number of small HSPs. In the present study we elucidate the role of U. maydis small HSPs in the pathogenicity as well as general stress response of the fungus. Through quantitative real time PCR analysis the expression levels of small HSP genes in comparison with other HSPs were assessed both during infection of the host plant Zea mays and when the pathogen was subjected to an abiotic stress such as oxidative stress. This study revealed that contrary to other HSPs, small HSPs showed an increased level of differential expression under both the tested conditions, indicating a possible role of small HSPs in the pathogenicity and stress response of U. maydis. This has been further confirmed by generation of deletion and complementation strains of three putative small HSPs.
Keywords	Ustilago zeae ; Zea mays ; abiotic stress ; fungi ; gene expression regulation ; genes ; heat shock proteins ; host plants ; oxidative stress ; pathogenesis ; pathogenicity ; pathogens ; quantitative polymerase chain reaction ; stress response
Language	English
Dates of publication	2014-12
Size	p. 17-24.
Publishing place	Published by Elsevier/North Holland on behalf of the Federation of European Microbiological Societies.
Document type	Article
Note	LETTER
ZDB-ID	752343-9
ISSN	1574-6968 ; 0378-1097
ISSN (online)	1574-6968
ISSN	0378-1097
DOI	10.1111/1574-6968.12605
Database	NAL-Catalogue (AGRICOLA)

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Zs.A 1372: Show issues

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Article ; Online: Insight into the biochemical and cell biological function of an intrinsically unstructured heat shock protein, Hsp12 of Ustilago maydis.

Mitra, Aroni / Bhakta, Koustav / Kar, Ankita / Roy, Anisha / Mohid, Sk Abdul / Ghosh, Abhrajyoti / Ghosh, Anupama

Molecular plant pathology

2023 Volume 24, Issue 9, Page(s) 1063–1077

Abstract	Small heat shock proteins (sHsps) play diverse roles in the stress response and maintenance of cellular functions. The Ustilago maydis genome codes for few sHsps. Among these, Hsp12 has previously been demonstrated to be involved in the pathogenesis of the fungus by our group. In the present study we further investigated the biological function of the protein in the pathogenic development of U. maydis. Analysis of the primary amino acid sequence of Hsp12 in combination with spectroscopic methods to analyse secondary protein structures revealed an intrinsically disordered nature of the protein. We also carried out detailed analysis on the protein aggregation prevention activity associated with Hsp12. Our data suggest Hsp12 has trehalose-dependent protein aggregation prevention activity. Through assaying the interaction of Hsp12 with lipid membranes in vitro we also showed the ability of U. maydis Hsp12 to induce stability in lipid vesicles. U. maydis hsp12 deletion mutants exhibited defects in the endocytosis process and delayed completion of the pathogenic life cycle. Therefore, U. maydis Hsp12 contributes to the pathogenic development of the fungus through its ability to relieve proteotoxic stress during infection as well as its membrane-stabilizing function.
MeSH term(s)	Heat-Shock Proteins/genetics ; Heat-Shock Proteins/metabolism ; Protein Aggregates ; Basidiomycota/metabolism ; Ustilago/genetics ; Ustilago/metabolism ; Lipids ; Fungal Proteins/genetics ; Fungal Proteins/metabolism
Chemical Substances	Heat-Shock Proteins ; Protein Aggregates ; Lipids ; Fungal Proteins
Language	English
Publishing date	2023-07-11
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020755-4
ISSN	1364-3703 ; 1364-3703
ISSN (online)	1364-3703
ISSN	1364-3703
DOI	10.1111/mpp.13350
Database	MEDical Literature Analysis and Retrieval System OnLINE

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Article ; Online: Chemical leukoderma due to hydroquinone: An unusual phenomenon.

Das, Anupam / Ghosh, Anupama / Kumar, Piyush

Indian journal of dermatology, venereology and leprology

2019 Volume 85, Issue 5, Page(s) 567

MeSH term(s)	Adult ; Facial Dermatoses/chemically induced ; Facial Dermatoses/pathology ; Female ; Humans ; Hydroquinones/adverse effects ; Hypopigmentation/chemically induced ; Hypopigmentation/pathology ; Melanosis/drug therapy ; Self Medication/adverse effects ; Skin Lightening Preparations/adverse effects
Chemical Substances	Hydroquinones ; Skin Lightening Preparations ; hydroquinone (XV74C1N1AE)
Language	English
Publishing date	2019-01-17
Publishing country	India
Document type	Case Reports ; Letter
ZDB-ID	416068-x
ISSN	0973-3922 ; 0019-5162 ; 0378-6323
ISSN (online)	0973-3922
ISSN	0019-5162 ; 0378-6323
DOI	10.4103/ijdvl.IJDVL_209_17
Database	MEDical Literature Analysis and Retrieval System OnLINE

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