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Proteomic analysis reveals metabolic and regulatory systems involved in the syntrophic and axenic lifestyle of Syntrophomonas wolfei.

Frontiers in microbiology

Sieber JR, Crable BR, Sheik CS, Hurst GB, Rohlin L, Gunsalus RP, McInerney MJ.
PMID: 25717324
Front Microbiol. 2015 Feb 11;6:115. doi: 10.3389/fmicb.2015.00115. eCollection 2015.

Microbial syntrophy is a vital metabolic interaction necessary for the complete oxidation of organic biomass to methane in all-anaerobic ecosystems. However, this process is thermodynamically constrained and represents an ecosystem-level metabolic bottleneck. To gain insight into the physiology of...

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Sieber JR, Crable BR, Sheik CS, et al. Proteomic analysis reveals metabolic and regulatory systems involved in the syntrophic and axenic lifestyle of Syntrophomonas wolfei. Front Microbiol. 2015;6:115doi: 10.3389/fmicb.2015.00115.
Sieber, J. R., Crable, B. R., Sheik, C. S., Hurst, G. B., Rohlin, L., Gunsalus, R. P., & McInerney, M. J. (2015). Proteomic analysis reveals metabolic and regulatory systems involved in the syntrophic and axenic lifestyle of Syntrophomonas wolfei. Frontiers in microbiology, 6115. https://doi.org/10.3389/fmicb.2015.00115
Sieber, Jessica R, et al. "Proteomic analysis reveals metabolic and regulatory systems involved in the syntrophic and axenic lifestyle of Syntrophomonas wolfei." Frontiers in microbiology vol. 6 (2015): 115. doi: https://doi.org/10.3389/fmicb.2015.00115
Sieber JR, Crable BR, Sheik CS, Hurst GB, Rohlin L, Gunsalus RP, McInerney MJ. Proteomic analysis reveals metabolic and regulatory systems involved in the syntrophic and axenic lifestyle of Syntrophomonas wolfei. Front Microbiol. 2015 Feb 11;6:115. doi: 10.3389/fmicb.2015.00115. eCollection 2015. PMID: 25717324; PMCID: PMC4324140.
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Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10.

Kinetoplastid biology and disease

Zamora-Veyl FB, Kroemer M, Zander D, Clos J.
PMID: 15862128
Kinetoplastid Biol Dis. 2005 Apr 29;4(1):3. doi: 10.1186/1475-9292-4-3.

BACKGROUND: Leishmania spp., in the course of their parasitic life cycle, encounter two vastly different environments: the gut of sandflies and the phagosomes of mammalian macrophages. During transmission into a mammal, the parasites are exposed to increased ambient temperature...

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Zamora-Veyl FB, Kroemer M, Zander D, et al. Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10. Kinetoplastid Biol Dis. 2005;4(1):3doi: 10.1186/1475-9292-4-3.
Zamora-Veyl, F. B., Kroemer, M., Zander, D., & Clos, J. (2005). Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10. Kinetoplastid biology and disease, 4(1), 3. https://doi.org/10.1186/1475-9292-4-3
Zamora-Veyl, Fanny Beatriz, et al. "Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10." Kinetoplastid biology and disease vol. 4,1 (2005): 3. doi: https://doi.org/10.1186/1475-9292-4-3
Zamora-Veyl FB, Kroemer M, Zander D, Clos J. Stage-specific expression of the mitochondrial co-chaperonin of Leishmania donovani, CPN10. Kinetoplastid Biol Dis. 2005 Apr 29;4(1):3. doi: 10.1186/1475-9292-4-3. PMID: 15862128; PMCID: PMC1097755.
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Opening up the group II chaperonins.

Structure (London, England : 1993)

Rao Z.
PMID: 20947006
Structure. 2010 Oct 13;18(10):1221-2. doi: 10.1016/j.str.2010.09.004.

A new study in this issue of Structure (Huo et al., 2010) reports the crystal structure of a group II chaperonin in the open state, providing unprecedented levels of detail for the domain movements that result from ATP hydrolysis...

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Rao Z. Opening up the group II chaperonins. Structure. 2010;18(10):1221-2doi: 10.1016/j.str.2010.09.004.
Rao, Z. (2010). Opening up the group II chaperonins. Structure (London, England : 1993), 18(10), 1221-2. https://doi.org/10.1016/j.str.2010.09.004
Rao, Zihe. "Opening up the group II chaperonins." Structure (London, England : 1993) vol. 18,10 (2010): 1221-2. doi: https://doi.org/10.1016/j.str.2010.09.004
Rao Z. Opening up the group II chaperonins. Structure. 2010 Oct 13;18(10):1221-2. doi: 10.1016/j.str.2010.09.004. PMID: 20947006.
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Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts.

Planta

Jāger KM, Bergman B.
PMID: 24193540
Planta. 1991 Dec;183(1):120-5. doi: 10.1007/BF00197575.

The occurrence and distribution of a multifunctional chaperonin-60 (cpn60), the GroEL protein, was demonstrated in the cyanobacterium Anabaena PCC 7120 by using a rabbit anti-GroEL (Escherichia coli) antibody. Western-blot analysis showed a distinct cross-reaction with a protein of approx....

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Jāger KM, Bergman B. Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta. 1991;183(1):120-5doi: 10.1007/BF00197575.
Jāger, K. M., & Bergman, B. (1991). Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta, 183(1), 120-5. https://doi.org/10.1007/BF00197575
Jāger, K M, and Bergman, B. "Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts." Planta vol. 183,1 (1991): 120-5. doi: https://doi.org/10.1007/BF00197575
Jāger KM, Bergman B. Localization of a multifunctional chaperonin (GroEL protein) in nitrogen-fixing Anabaena PCC 7120 : Presence in vegetative cells and heterocysts. Planta. 1991 Dec;183(1):120-5. doi: 10.1007/BF00197575. PMID: 24193540.
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Comprehensive Transcriptome Profiling and Identification of Potential Genes Responsible for Salt Tolerance in Tall Fescue Leaves under Salinity Stress.

Genes

Amombo E, Li X, Wang G, An S, Wang W, Fu J.
PMID: 30248970
Genes (Basel). 2018 Sep 21;9(10). doi: 10.3390/genes9100466.

Soil salinity is a serious threat to plant growth and crop productivity. Tall fescue utilization in saline areas is limited by its inferior salt tolerance. Thus, a transcriptome study is a prerequisite for future research aimed at providing deeper...

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Amombo E, Li X, Wang G, et al. Comprehensive Transcriptome Profiling and Identification of Potential Genes Responsible for Salt Tolerance in Tall Fescue Leaves under Salinity Stress. Genes (Basel). 2018;9(10)doi: 10.3390/genes9100466.
Amombo, E., Li, X., Wang, G., An, S., Wang, W., & Fu, J. (2018). Comprehensive Transcriptome Profiling and Identification of Potential Genes Responsible for Salt Tolerance in Tall Fescue Leaves under Salinity Stress. Genes, 9(10), . https://doi.org/10.3390/genes9100466
Amombo, Erick, et al. "Comprehensive Transcriptome Profiling and Identification of Potential Genes Responsible for Salt Tolerance in Tall Fescue Leaves under Salinity Stress." Genes vol. 9,10 (2018). doi: https://doi.org/10.3390/genes9100466
Amombo E, Li X, Wang G, An S, Wang W, Fu J. Comprehensive Transcriptome Profiling and Identification of Potential Genes Responsible for Salt Tolerance in Tall Fescue Leaves under Salinity Stress. Genes (Basel). 2018 Sep 21;9(10). doi: 10.3390/genes9100466. PMID: 30248970; PMCID: PMC6210376.
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Chaperonins: Nanocarriers with Biotechnological Applications.

Nanomaterials (Basel, Switzerland)

Pipaón S, Gragera M, Bueno-Carrasco MT, García-Bernalt Diego J, Cantero M, Cuéllar J, Fernández-Fernández MR, Valpuesta JM.
PMID: 33671209
Nanomaterials (Basel). 2021 Feb 17;11(2). doi: 10.3390/nano11020503.

Chaperonins are molecular chaperones found in all kingdoms of life, and as such they assist in the folding of other proteins. Structurally, chaperonins are cylinders composed of two back-to-back rings, each of which is an oligomer of ~60-kDa proteins....

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Pipaón S, Gragera M, Bueno-Carrasco MT, et al. Chaperonins: Nanocarriers with Biotechnological Applications. Nanomaterials (Basel). 2021;11(2)doi: 10.3390/nano11020503.
Pipaón, S., Gragera, M., Bueno-Carrasco, M. T., García-Bernalt Diego, J., Cantero, M., Cuéllar, J., Fernández-Fernández, M. R., & Valpuesta, J. M. (2021). Chaperonins: Nanocarriers with Biotechnological Applications. Nanomaterials (Basel, Switzerland), 11(2), . https://doi.org/10.3390/nano11020503
Pipaón, Sergio, et al. "Chaperonins: Nanocarriers with Biotechnological Applications." Nanomaterials (Basel, Switzerland) vol. 11,2 (2021). doi: https://doi.org/10.3390/nano11020503
Pipaón S, Gragera M, Bueno-Carrasco MT, García-Bernalt Diego J, Cantero M, Cuéllar J, Fernández-Fernández MR, Valpuesta JM. Chaperonins: Nanocarriers with Biotechnological Applications. Nanomaterials (Basel). 2021 Feb 17;11(2). doi: 10.3390/nano11020503. PMID: 33671209; PMCID: PMC7922521.
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Genome Wide Analysis of .

Iranian journal of biotechnology

Shafqat W, Jaskani MJ, Maqbool R, Sattar Khan A, Abbas Naqvi S, Ali Z, Ahmad Khan I.
PMID: 34056019
Iran J Biotechnol. 2020 Oct 01;18(4):e2529. doi: 10.30498/IJB.2020.2529. eCollection 2020 Oct.

BACKGROUND: Plant and animal cells possess a ubiquitous protein known as heat shock proteins (HSPs). Hsps were originally described in relation to heat shock and against abiotic and biotic stresses. Heat shock protein was classified in other crops on...

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Shafqat W, Jaskani MJ, Maqbool R, et al. Genome Wide Analysis of . Iran J Biotechnol. 2020;18(4):e2529doi: 10.30498/IJB.2020.2529.
Shafqat, W., Jaskani, M. J., Maqbool, R., Sattar Khan, A., Abbas Naqvi, S., Ali, Z., & Ahmad Khan, I. (2020). Genome Wide Analysis of . Iranian journal of biotechnology, 18(4), e2529. https://doi.org/10.30498/IJB.2020.2529
Shafqat, Waqar, et al. "Genome Wide Analysis of ." Iranian journal of biotechnology vol. 18,4 (2020): e2529. doi: https://doi.org/10.30498/IJB.2020.2529
Shafqat W, Jaskani MJ, Maqbool R, Sattar Khan A, Abbas Naqvi S, Ali Z, Ahmad Khan I. Genome Wide Analysis of . Iran J Biotechnol. 2020 Oct 01;18(4):e2529. doi: 10.30498/IJB.2020.2529. eCollection 2020 Oct. PMID: 34056019; PMCID: PMC8148642.
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Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation.

Veterinary microbiology

Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ.
PMID: 34826648
Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10.

Avian reoviruses (ARVs) are important pathogens that cause considerable economic losses in poultry farming. To date, host factors that control stabilization of ARV proteins remain largely unknown. In this work we determined that the eukaryotic chaperonin T-complex protein-1 (TCP-1)...

Cite
Huang WR, Li JY, Liao TL, et al. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021;264:109277doi: 10.1016/j.vetmic.2021.109277.
Huang, W. R., Li, J. Y., Liao, T. L., Yeh, C. M., Wang, C. Y., Wen, H. W., Hu, N. J., Wu, Y. Y., Hsu, C. Y., Chang, Y. K., Chang, C. D., Nielsen, B. L., & Liu, H. J. (2021). Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Veterinary microbiology, 264109277. https://doi.org/10.1016/j.vetmic.2021.109277
Huang, Wei-Ru, et al. "Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation." Veterinary microbiology vol. 264 (2021): 109277. doi: https://doi.org/10.1016/j.vetmic.2021.109277
Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10. PMID: 34826648.
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Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation.

Veterinary microbiology

Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ.
PMID: 34826648
Vet Microbiol. 2022 Jan;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10.

Avian reoviruses (ARVs) are important pathogens that cause considerable economic losses in poultry farming. To date, host factors that control stabilization of ARV proteins remain largely unknown. In this work we determined that the eukaryotic chaperonin T-complex protein-1 (TCP-1)...

Cite
Huang WR, Li JY, Liao TL, et al. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021;264:109277doi: 10.1016/j.vetmic.2021.109277.
Huang, W. R., Li, J. Y., Liao, T. L., Yeh, C. M., Wang, C. Y., Wen, H. W., Hu, N. J., Wu, Y. Y., Hsu, C. Y., Chang, Y. K., Chang, C. D., Nielsen, B. L., & Liu, H. J. (2022). Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Veterinary microbiology, 264109277. https://doi.org/10.1016/j.vetmic.2021.109277
Huang, Wei-Ru, et al. "Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation." Veterinary microbiology vol. 264 (2022): 109277. doi: https://doi.org/10.1016/j.vetmic.2021.109277
Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2022 Jan;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10. PMID: 34826648.
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The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES.

Microbiology spectrum

Houghton J, Rodgers A, Rose G, D'Halluin A, Kipkorir T, Barker D, Waddell SJ, Arnvig KB.
PMID: 34549992
Microbiol Spectr. 2021 Oct 31;9(2):e0109521. doi: 10.1128/Spectrum.01095-21. Epub 2021 Sep 22.

Almost 140 years after the identification of Mycobacterium tuberculosis as the etiological agent of tuberculosis, important aspects of its biology remain poorly described. Little is known about the role of posttranscriptional control of gene expression and RNA biology, including...

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Houghton J, Rodgers A, Rose G, et al. The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES. Microbiol Spectr. 2021;9(2):e0109521doi: 10.1128/Spectrum.01095-21.
Houghton, J., Rodgers, A., Rose, G., D'Halluin, A., Kipkorir, T., Barker, D., Waddell, S. J., & Arnvig, K. B. (2021). The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES. Microbiology spectrum, 9(2), e0109521. https://doi.org/10.1128/Spectrum.01095-21
Houghton, Joanna, et al. "The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES." Microbiology spectrum vol. 9,2 (2021): e0109521. doi: https://doi.org/10.1128/Spectrum.01095-21
Houghton J, Rodgers A, Rose G, D'Halluin A, Kipkorir T, Barker D, Waddell SJ, Arnvig KB. The Mycobacterium tuberculosis sRNA F6 Modifies Expression of Essential Chaperonins, GroEL2 and GroES. Microbiol Spectr. 2021 Oct 31;9(2):e0109521. doi: 10.1128/Spectrum.01095-21. Epub 2021 Sep 22. PMID: 34549992; PMCID: PMC8557902.
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Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation.

Veterinary microbiology

Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ.
PMID: 34826648
Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10.

Avian reoviruses (ARVs) are important pathogens that cause considerable economic losses in poultry farming. To date, host factors that control stabilization of ARV proteins remain largely unknown. In this work we determined that the eukaryotic chaperonin T-complex protein-1 (TCP-1)...

Cite
Huang WR, Li JY, Liao TL, et al. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021;264:109277doi: 10.1016/j.vetmic.2021.109277.
Huang, W. R., Li, J. Y., Liao, T. L., Yeh, C. M., Wang, C. Y., Wen, H. W., Hu, N. J., Wu, Y. Y., Hsu, C. Y., Chang, Y. K., Chang, C. D., Nielsen, B. L., & Liu, H. J. (2021). Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Veterinary microbiology, 264109277. https://doi.org/10.1016/j.vetmic.2021.109277
Huang, Wei-Ru, et al. "Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation." Veterinary microbiology vol. 264 (2021): 109277. doi: https://doi.org/10.1016/j.vetmic.2021.109277
Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10. PMID: 34826648.
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Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation.

Veterinary microbiology

Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ.
PMID: 34826648
Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10.

Avian reoviruses (ARVs) are important pathogens that cause considerable economic losses in poultry farming. To date, host factors that control stabilization of ARV proteins remain largely unknown. In this work we determined that the eukaryotic chaperonin T-complex protein-1 (TCP-1)...

Cite
Huang WR, Li JY, Liao TL, et al. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021;264:109277doi: 10.1016/j.vetmic.2021.109277.
Huang, W. R., Li, J. Y., Liao, T. L., Yeh, C. M., Wang, C. Y., Wen, H. W., Hu, N. J., Wu, Y. Y., Hsu, C. Y., Chang, Y. K., Chang, C. D., Nielsen, B. L., & Liu, H. J. (2021). Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Veterinary microbiology, 264109277. https://doi.org/10.1016/j.vetmic.2021.109277
Huang, Wei-Ru, et al. "Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation." Veterinary microbiology vol. 264 (2021): 109277. doi: https://doi.org/10.1016/j.vetmic.2021.109277
Huang WR, Li JY, Liao TL, Yeh CM, Wang CY, Wen HW, Hu NJ, Wu YY, Hsu CY, Chang YK, Chang CD, Nielsen BL, Liu HJ. Molecular chaperone TRiC governs avian reovirus replication by protecting outer-capsid protein σC and inner core protein σA and non-structural protein σNS from ubiquitin- proteasome degradation. Vet Microbiol. 2021 Nov 10;264:109277. doi: 10.1016/j.vetmic.2021.109277. Epub 2021 Nov 10. PMID: 34826648.
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