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Kieselbach, Thomas
Publications (10 of 48) Show all publications
Gomez, F. M., Carrion, C. A., Costa, M. L., Desel, C., Kieselbach, T., Funk, C., . . . Guiamet, J. (2019). Extra-plastidial degradation of chlorophyll and photosystem I in tobacco leaves involving 'senescence-associated vacuoles'. The Plant Journal, 99(3), 465-477
Open this publication in new window or tab >>Extra-plastidial degradation of chlorophyll and photosystem I in tobacco leaves involving 'senescence-associated vacuoles'
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2019 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 99, no 3, p. 465-477Article in journal (Refereed) Published
Abstract [en]

Chlorophyll (Chl) loss is the main visible symptom of senescence in leaves. The initial steps of Chl degradation operate within the chloroplast, but the observation that ‘senescence‐associated vacuoles’ (SAVs) contain Chl raises the question of whether SAVs might also contribute to Chl breakdown. Previous confocal microscope observations (Martínez et al., 2008) showed many SAVs containing Chl. Isolated SAVs contained Chl a and b (with a Chl a/b ratio close to 5) and lower levels of chlorophyllide a. Pheophytin a and pheophorbide a were formed after the incubation of SAVs at 30°C in darkness, suggesting the presence of Chl‐degrading activities in SAVs. Chl in SAVs was bound to a number of ‘green bands’. In the most abundant green band of SAVs, Western blot analysis showed the presence of photosystem I (PSI) Chl‐binding proteins, including the PsaA protein of the PSI reaction center and the apoproteins of the light‐harvesting complexes (Lhca 1–4). This was confirmed by: (i) measurements of 77‐K fluorescence emission spectra showing a single emission peak at around 730 nm in SAVs; (ii) mass spectrometry of the most prominent green band with the slowest electrophoretic mobility; and (iii) immunofluorescence detection of PsaA in SAVs observed through confocal microscopy. Incubation of SAVs at 30°C in darkness caused a steady decrease in PsaA levels. Overall, these results indicate that SAVs may be involved in the degradation of PSI proteins and their associated chlorophylls during the senescence of leaves.

Place, publisher, year, edition, pages
John Wiley & Sons, 2019
Keywords
senescence-associated vacuoles, photosystem I, chlorophyll degradation, tobacco, Nicotiana tabacum
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-162399 (URN)10.1111/tpj.14337 (DOI)000477680000007 ()30985038 (PubMedID)2-s2.0-85066909992 (Scopus ID)
Available from: 2019-08-19 Created: 2019-08-19 Last updated: 2019-08-19Bibliographically approved
Gomez, F. M., Carrion, C. A., Costa, M. L., Desel, C., Kieselbach, T., Funk, C., . . . Guiamet, J. (2019). Extra-plastidial degradation of chlorophyll and photosystem I in tobacco leaves involving 'senescence-associated vacuoles'. The Plant Journal, 99(3), 465-477
Open this publication in new window or tab >>Extra-plastidial degradation of chlorophyll and photosystem I in tobacco leaves involving 'senescence-associated vacuoles'
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2019 (English)In: The Plant Journal, ISSN 0960-7412, E-ISSN 1365-313X, Vol. 99, no 3, p. 465-477Article in journal (Refereed) Published
Abstract [en]

Chlorophyll (Chl) loss is the main visible symptom of senescence in leaves. The initial steps of Chl degradation operate within the chloroplast, but the observation that 'senescence-associated vacuoles' (SAVs) contain Chl raises the question of whether SAVs might also contribute to Chl breakdown. Previous confocal microscope observations (Martinez et al., 2008) showed many SAVs containing Chl. Isolated SAVs contained Chl a and b (with a Chl a/b ratio close to 5) and lower levels of chlorophyllide a. Pheophytin a and pheophorbide a were formed after the incubation of SAVs at 30 degrees C in darkness, suggesting the presence of Chl-degrading activities in SAVs. Chl in SAVs was bound to a number of 'green bands'. In the most abundant green band of SAVs, Western blot analysis showed the presence of photosystem I (PSI) Chl-binding proteins, including the PsaA protein of the PSI reaction center and the apoproteins of the light-harvesting complexes (Lhca 1-4). This was confirmed by: (i) measurements of 77-K fluorescence emission spectra showing a single emission peak at around 730 nm in SAVs; (ii) mass spectrometry of the most prominent green band with the slowest electrophoretic mobility; and (iii) immunofluorescence detection of PsaA in SAVs observed through confocal microscopy. Incubation of SAVs at 30 degrees C in darkness caused a steady decrease in PsaA levels. Overall, these results indicate that SAVs may be involved in the degradation of PSI proteins and their associated chlorophylls during the senescence of leaves.

Place, publisher, year, edition, pages
WILEY, 2019
Keywords
senescence-associated vacuoles, photosystem I, chlorophyll degradation, tobacco, Nicotiana tabacum
National Category
Plant Biotechnology
Identifiers
urn:nbn:se:umu:diva-162317 (URN)10.1111/tpj.14337 (DOI)000477680000007 ()30985038 (PubMedID)
Available from: 2019-09-03 Created: 2019-09-03 Last updated: 2019-09-03Bibliographically approved
Kieselbach, T., Cheregi, O., Green, B. R. & Funk, C. (2018). Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities. Photosynthesis Research, 135(1–3), 149-163
Open this publication in new window or tab >>Proteomic analysis of the phycobiliprotein antenna of the cryptophyte alga Guillardia theta cultured under different light intensities
2018 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 135, no 1–3, p. 149-163Article in journal (Refereed) Published
Abstract [en]

Plants and algae have developed various light-harvesting mechanisms for optimal delivery of excitation energy to the photosystems. Cryptophyte algae have evolved a novel soluble light-harvesting antenna utilizing phycobilin pigments to complement the membrane-intrinsic Chl a/c-binding LHC antenna. This new antenna consists of the plastid-encoded β-subunit, a relic of the ancestral phycobilisome, and a novel nuclear-encoded α-subunit unique to cryptophytes. Together, these proteins form the active α1β·α2β-tetramer. In all cryptophyte algae investigated so far, the α-subunits have duplicated and diversified into a large gene family. Although there is transcriptional evidence for expression of all these genes, the X-ray structures determined to date suggest that only two of the α-subunit genes might be significantly expressed at the protein level. Using proteomics, we show that in phycoerythrin 545 (PE545) of Guillardia theta, the only cryptophyte with a sequenced genome, all 20 α-subunits are expressed when the algae grow under white light. The expression level of each protein depends on the intensity of the growth light, but there is no evidence for a specific light-dependent regulation of individual members of the α-subunit family under the growth conditions applied. GtcpeA10 seems to be a special member of the α-subunit family, because it consists of two similar N- and C-terminal domains, which likely are the result of a partial tandem gene duplication. The proteomics data of this study have been deposited to the ProteomeXchange Consortium and have the dataset identifiers PXD006301 and 10.6019/PXD006301.

Place, publisher, year, edition, pages
Springer, 2018
Keywords
Cryptophyta, Phycobilin, Phycobiliprotein, Translation, TAT-pathway, Proteomics
National Category
Biochemistry and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-143747 (URN)10.1007/s11120-017-0400-0 (DOI)000423338500016 ()28540588 (PubMedID)
Available from: 2018-01-08 Created: 2018-01-08 Last updated: 2018-06-09Bibliographically approved
Kieselbach, T. & Oscarsson, J. (2017). Dataset of the proteome of purified outer membrane vesicles from the human pathogen Aggregatibacter actinomycetemcomintans. Data in Brief, 10, 426-431
Open this publication in new window or tab >>Dataset of the proteome of purified outer membrane vesicles from the human pathogen Aggregatibacter actinomycetemcomintans
2017 (English)In: Data in Brief, ISSN 2352-3409, Vol. 10, p. 426-431Article in journal (Refereed) Published
Abstract [en]

Abstract The Gram-negative bacterium Aggregatibacter actinomycetemcomitans is an oral and systemic pathogen, which is linked to aggressive forms of periodontitis and can be associated with endocarditis. The outer membrane vesicles (OMVs) of this species contain effector proteins such as cytolethal distending toxin (CDT) and leukotoxin (LtxA), which they can deliver into human host cells. The OMVs can also activate innate immunity through NOD1- and NOD2-active pathogen-associated molecular patterns. This dataset provides a proteome of highly purified OMVs from A. actinomycetemcomitans serotype e strain 173. The experimental data do not only include the raw data of the LC-MS/MS analysis of four independent preparations of purified OMVs but also the mass lists of the processed data and the Mascot.dat files from the database searches. In total 501 proteins are identified, of which 151 are detected in at least three of four independent preparations. In addition, this dataset contains the COG definitions and the predicted subcellular locations (PSORTb 3.0) for the entire genome of A. actinomycetemcomitans serotype e strain SC1083, which is used for the evaluation of the LC-MS/MS data. These data are deposited in ProteomeXchange in the public dataset PXD002509. In addition, a scientific interpretation of this dataset by Kieselbach et al. (2015) [2] is available at http://dx.doi.org/10.1371/journal.pone.0138591.

Place, publisher, year, edition, pages
Elsevier, 2017
Keywords
Micobiology, Odontology, Periodontitis, Outer membrane vesicle, Proteomics
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-128946 (URN)10.1016/j.dib.2016.12.015 (DOI)28050585 (PubMedID)
Available from: 2016-12-20 Created: 2016-12-20 Last updated: 2018-06-09Bibliographically approved
Kieselbach, T., Zijnge, V., Granström, E. & Oscarsson, J. (2015). Proteomics of Aggregatibacter actinomycetemcomitans Outer Membrane Vesicles. PLoS ONE, 10(9), Article ID e0138591.
Open this publication in new window or tab >>Proteomics of Aggregatibacter actinomycetemcomitans Outer Membrane Vesicles
2015 (English)In: PLoS ONE, ISSN 1932-6203, E-ISSN 1932-6203, Vol. 10, no 9, article id e0138591Article in journal (Refereed) Published
Abstract [en]

Aggregatibacter actinomycetemcomitans is an oral and systemic pathogen associated with aggressive forms of periodontitis and with endocarditis. Outer membrane vesicles (OMVs) released by this species have been demonstrated to deliver effector proteins such as cytolethal distending toxin (CDT) and leukotoxin (LtxA) into human host cells and to act as triggers of innate immunity upon carriage of NOD1- and NOD2-active pathogen-associated molecular patterns (PAMPs). To improve our understanding of the pathogenicity-associated functions that A. actinomycetemcomitans exports via OMVs, we studied the proteome of density gradient-purified OMVs from a rough-colony type clinical isolate, strain 173 (serotype e) using liquid chromatography-tandem mass spectrometry (LC-MS/MS). This analysis yielded the identification of 151 proteins, which were found in at least three out of four independent experiments. Data are available via ProteomeXchange with identifier PXD002509. Through this study, we not only confirmed the vesicle-associated release of LtxA, and the presence of proteins, which are known to act as immunoreactive antigens in the human host, but we also identified numerous additional putative virulence-related proteins in the A. actinomycetemcomitans OMV proteome. The known and putative functions of these proteins include immune evasion, drug targeting, and iron/nutrient acquisition. In summary, our findings are consistent with an OMV-associated proteome that exhibits several offensive and defensive functions, and they provide a comprehensive basis to further disclose roles of A. actinomycetemcomitans OMVs in periodontal and systemic disease.

National Category
Medical and Health Sciences Clinical Medicine
Identifiers
urn:nbn:se:umu:diva-110086 (URN)10.1371/journal.pone.0138591 (DOI)000361790200135 ()26381655 (PubMedID)
Available from: 2015-10-15 Created: 2015-10-15 Last updated: 2018-06-07Bibliographically approved
Agrawal, G. K., Job, D., Kieselbach, T., Barkla, B. J., Chen, S., Deswal, R., . . . Rakwal, R. (2013). INPPO Actions and Recognition as a Driving Force for Progress in Plant Proteomics: Change of Guard, INPPO Update, and Upcoming Activities. Proteomics, 13(21), 3093-3100
Open this publication in new window or tab >>INPPO Actions and Recognition as a Driving Force for Progress in Plant Proteomics: Change of Guard, INPPO Update, and Upcoming Activities
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2013 (English)In: Proteomics, ISSN 1615-9853, E-ISSN 1615-9861, Vol. 13, no 21, p. 3093-3100Article in journal (Other academic) Published
Abstract [en]

The International Plant Proteomics Organization (INPPO) is a non-profit organization whose members are scientists involved or interested in plant proteomics. Since the publication of the first INPPO highlights in 2012, continued progress on many of the organization's mandates/goals has been achieved. Two major events are emphasized in this second INPPO highlights. First, the change of guard at the top, passing of the baton from Dominique Job, INPPO founding President to Ganesh Kumar Agrawal as the incoming President. Ganesh K. Agrawal, along with Dominique Job and Randeep Rakwal initiated the INPPO. Second, the most recent INPPO achievements and future targets, mainly the organization of first the INPPO World Congress in 2014, tentatively planned for Hamburg (Germany), are mentioned.

Keywords
INPPO, Newsletter, Plant proteomics, Conference
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-86630 (URN)10.1002/pmic.201370167 (DOI)000330251700001 ()
Available from: 2014-04-30 Created: 2014-03-03 Last updated: 2018-06-07Bibliographically approved
Haniewicz, P., De Sanctis, D., Büchel, C., Schröder, W. P., Loi, M. C., Kieselbach, T., . . . Piano, D. (2013). Isolation of monomeric photosystem II that retains the subunit PsbS.. Photosynthesis Research, 118(3), 199-207
Open this publication in new window or tab >>Isolation of monomeric photosystem II that retains the subunit PsbS.
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2013 (English)In: Photosynthesis Research, ISSN 0166-8595, E-ISSN 1573-5079, Vol. 118, no 3, p. 199-207Article in journal (Refereed) Published
Abstract [en]

Photosystem II has been purified from a transplastomic strain of Nicotiana tabacum according to two different protocols. Using the procedure described in Piano et al. (Photosynth Res 106:221-226, 2010) it was possible to isolate highly active PSII composed of monomers and dimers but depleted in their PsbS protein content. A "milder" procedure than the protocol reported by Fey et al. (Biochim Biophys Acta 1777:1501-1509, 2008) led to almost exclusively monomeric PSII complexes which in part still bind the PsbS protein. This finding might support a role for PSII monomers in higher plants.

Place, publisher, year, edition, pages
Springer, 2013
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-82591 (URN)10.1007/s11120-013-9914-2 (DOI)23975205 (PubMedID)
Available from: 2013-11-05 Created: 2013-11-05 Last updated: 2018-06-08Bibliographically approved
Kieselbach, T. (2013). Oxidative folding in chloroplasts. Antioxidants and Redox Signaling, 19(1), 72-82
Open this publication in new window or tab >>Oxidative folding in chloroplasts
2013 (English)In: Antioxidants and Redox Signaling, ISSN 1523-0864, E-ISSN 1557-7716, Vol. 19, no 1, p. 72-82Article in journal (Refereed) Published
Abstract [en]

Significance: Disulfide-bonded proteins in chloroplasts from green plants exist in the envelope and the thylakoid membrane, and in the stroma and the lumen. The formation of disulfide bonds in proteins is referred to as oxidative folding and is linked to the import and folding of chloroplast proteins as well as the assembly and repair of thylakoid complexes. It is also important in the redox regulation of enzymes and signal transfer.

Recent Advances: Green-plant chloroplasts contain enzymes that can form and isomerize disulfide bonds in proteins. In Arabidopsis thaliana, four proteins are identified that are relevant for the catalysis of disulfide bond formation in chloroplast proteins. The proteins' low quantum yield of Photosystem II 1 (LQY1, At1g75690) and snowy cotyledon 2 (SCO2, At3g19220) exhibits protein disulfide isomerase activity and is suggested to function in the assembly and repair of Photosystem II (PSII), and the biogenesis of thylakoids in cotyledons, respectively. The thylakoid-located Lumen thiol oxidoreductase 1 (LTO1, At4g35760) can catalyze the formation of the disulfide bond of the extrinsic PsbO protein of PSII. In addition, the stroma-located protein disulfide isomerase PDIL1-3 (At3g54960) may have a role in oxidative folding.

Critical Issues: Research on oxidative folding in chloroplasts plants is in an early stage and little is known about the mechanisms of disulfide bond formation in chloroplast proteins.

Future Directions: The close link between the import and folding of chloroplast proteins suggests that Hsp93, a component of the inner envelope's import apparatus, may have co-chaperones that can catalyze disulfide bond formation in newly imported proteins.

Place, publisher, year, edition, pages
New Rochelle: Mary Ann Liebert, 2013
Keywords
protein disulfide isomerase, K epoxide reductase, biogenesis factor CYO1, thylakoid lumen, arabidopsis thaliana, plastidial thioredoxins, tobacco chloroplasts, envelope membrane, escherichia coli, glutaredoxin S12
National Category
Biological Sciences
Identifiers
urn:nbn:se:umu:diva-65833 (URN)10.1089/ars.2012.4582 (DOI)000320029700008 ()23289792 (PubMedID)
Available from: 2013-02-12 Created: 2013-02-12 Last updated: 2018-06-08Bibliographically approved
Agrawal, G. K., Sarkar, A., Agrawal, R., Ndimba, B. K., Tanou, G., Dunn, M. J., . . . Rakwal, R. (2012). Boosting the Globalization of Plant Proteomics through INPPO: Current Developments and Future Prospects. Proteomics, 12(3), 359-368
Open this publication in new window or tab >>Boosting the Globalization of Plant Proteomics through INPPO: Current Developments and Future Prospects
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2012 (English)In: Proteomics, ISSN 1615-9853, E-ISSN 1615-9861, Vol. 12, no 3, p. 359-368Article in journal (Refereed) Published
Abstract [en]

The International Plant Proteomics Organization (INPPO) is a non-profit-organization consisting of people who are involved or interested in plant proteomics. INPPO is constantly growing in volume and activity, which is mostly due to the realization among plant proteomics researchers worldwide for the need of such a global platform. Their active participation resulted in the rapid growth within the first year of INPPO's official launch in 2011 via its website (www.inppo.com) and publication of the 'Viewpoint paper' in a special issue of PROTEOMICS (May 2011). Here, we will be highlighting the progress achieved in the year 2011 and the future targets for the year 2012 and onwards. INPPO has achieved a successful administrative structure, the Core Committee (CC; composed of President, Vice-President, and General Secretaries), Executive Council (EC), and General Body (GB) to achieve INPPO objectives. Various committees and subcommittees are in the process of being functionalized via discussion amongst scientists around the globe. INPPO's primary aim to popularize the plant proteomics research in biological sciences has also been recognized by PROTEOMICS where a section dedicated to plant proteomics has been introduced starting January 2012, following the very first issue of this journal devoted to plant proteomics in May 2011. To disseminate organizational activities to the scientific community, INPPO has launched a biannual (in January and July) newsletter entitled 'INPPO Express: News & Views' with the first issue published in January 2012. INPPO is also planning to have several activities in 2012, including programs within the Education Outreach committee in different countries, and the development of research ideas and proposals with priority on crop and horticultural plants, while keeping tight interactions with proteomics programs on model plants such as Arabidopsis thaliana, rice, and Medicago truncatula. Altogether, the INPPO progress and upcoming activities are because of immense support, dedication, and hard work of all members of the INPPO community, and also due to the wide encouragement and support from the communities (scientific and non-scientific).

Keywords
Crops, INPPO, Model plants, Plant proteomics, Tutorial
National Category
Cell and Molecular Biology
Identifiers
urn:nbn:se:umu:diva-52531 (URN)10.1002/pmic.201290018 (DOI)22290804 (PubMedID)
Available from: 2012-02-24 Created: 2012-02-24 Last updated: 2018-06-08Bibliographically approved
Jun, H., Kieselbach, T. & Jönsson, L. J. (2012). Comparative proteome analysis of Saccharomyces cerevisiae: A global overview of in vivo targets of the yeast activator protein 1. BMC Genomics, 13(1), 230
Open this publication in new window or tab >>Comparative proteome analysis of Saccharomyces cerevisiae: A global overview of in vivo targets of the yeast activator protein 1
2012 (English)In: BMC Genomics, ISSN 1471-2164, E-ISSN 1471-2164, Vol. 13, no 1, p. 230-Article in journal (Refereed) Published
Abstract [en]

BACKGROUND: : The activity of the yeast activator protein 1 (Yap1p) increases under stress conditions, which leads to enhanced transcription of a number of genes encoding protective enzymes or other proteins. To obtain a global overview of changes in expression of Yap1p-targeted proteins, we compared a Yap1p-overexpressing transformant with a control transformant by triplicate analysis of the proteome using two-dimensional gel electrophoresis (2-DE). Proteins of interest were identified using MALDI-MS or LC-MS/MS. RESULTS: : The relative quantities of 55 proteins were elevated significantly upon overexpression of Yap1p, and most of these proteins were found to have a Yap1p-binding site upstream of their coding sequences. Interestingly, the main metabolic enzymes in the glycolysis and pyruvate-ethanol pathways showed a significant increase in the Yap1p-overexpressing transformant. Moreover, a comparison of our proteome data with transcriptome data from the literature suggested which proteins were regulated at the level of the proteome, and which proteins were regulated at the level of the transcriptome. Eight proteins involved in stress response, including seven heat-shock and chaperone proteins, were significantly more abundant in the Yap1p-overexpressing transformant. CONCLUSIONS: : We have investigated the general protein composition in Yap1p-overexpressing S. cerevisiae using proteomic techniques, and quantified the changes in the expression of the potential Yap1p-targeted proteins. Identification of the potential Yap1p targets and analysis of their role in cellular processes not only give a global overview of the ubiquitous cellular changes elicited by Yap1p, but also provide the framework for understanding the mechanisms behind Yap1p-regulated stress response in yeast.

Place, publisher, year, edition, pages
London: BioMed Central, 2012
Keywords
Yap1, Saccharomyces cerevisiae, Transcription factor, Stress response, Proteome
National Category
Chemical Sciences
Identifiers
urn:nbn:se:umu:diva-56351 (URN)10.1186/1471-2164-13-230 (DOI)000307947300001 ()22681880 (PubMedID)
Available from: 2012-06-14 Created: 2012-06-14 Last updated: 2018-06-08Bibliographically approved
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