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4. GTP binding to the ROC domain of DAP-kinase regulates its function through intramolecular signalling

Author

Carlessi, Rodrigo, Levin-Salomon, V., Ciprut, S., Bialik, S., Berissi, H., Albeck, S., Peleg, Y., Kimchi, A., Carlessi, Rodrigo, Levin-Salomon, V., Ciprut, S., Bialik, S., Berissi, H., Albeck, S., Peleg, Y., and Kimchi, A.

Abstract

Death-associated protein kinase (DAPk) was recently suggested by sequence homology to be a member of the ROCO family of proteins. Here, we show that DAPk has a functional ROC (Ras of complex proteins) domain that mediates homo-oligomerization and GTP binding through a defined P-loop motif. Upon binding to GTP, the ROC domain negatively regulates the catalytic activity of DAPk and its cellular effects. Mechanistically, GTP binding enhances an inhibitory autophosphorylation at a distal site that suppresses kinase activity. This study presents a new mechanism of intramolecular signal transduction, by which GTP binding operates in cis to affect the catalytic activity of a distal domain in the protein. © 2011 European Molecular Biology Organization.

Published
2011

5. Application of the use of high-throughput technologies to the determination of protein structures of bacterial and viral pathogens

Author

Fogg, M. J., Alzari, P., Bahar, M., Bertini, I., Betton, J. M., Burmeister, W. P., Cambillau, C., Canard, B., Carrondo, M., Coll, M., Daenke, S., Dym, O., Egloff, M. P., Enguita, F. J., Geerlof, A., Haouz, A., Jones, T. Alwyn, Ma, Qingjun, Manicka, S. N., Migliardi, M., Nordlund, P., Owens, R. J., Peleg, Y., Schneider, G., Schnell, R., Stuart, D. I., Tarbouriech, N., Unge, Torsten, Wilkinson, A. J., Wilmanns, M., Wilson, K. S., Zimhony, O., Grimes, J. M., Fogg, M. J., Alzari, P., Bahar, M., Bertini, I., Betton, J. M., Burmeister, W. P., Cambillau, C., Canard, B., Carrondo, M., Coll, M., Daenke, S., Dym, O., Egloff, M. P., Enguita, F. J., Geerlof, A., Haouz, A., Jones, T. Alwyn, Ma, Qingjun, Manicka, S. N., Migliardi, M., Nordlund, P., Owens, R. J., Peleg, Y., Schneider, G., Schnell, R., Stuart, D. I., Tarbouriech, N., Unge, Torsten, Wilkinson, A. J., Wilmanns, M., Wilson, K. S., Zimhony, O., and Grimes, J. M.

Abstract

The Structural Proteomics In Europe (SPINE) programme is aimed at the development and implementation of high-throughput technologies for the efficient structure determination of proteins of biomedical importance, such as those of bacterial and viral pathogens linked to human health. Despite the challenging nature of some of these targets, 175 novel pathogen protein structures (approximately 220 including complexes) have been determined to date. Here the impact of several technologies on the structural determination of proteins from human pathogens is illustrated with selected examples, including the parallel expression of multiple constructs, the use of standardized refolding protocols and optimized crystallization screens.

Published
2006
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6. Eukaryotic expression:Developments for structural proteomics

Author

Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Abstract

The production of sufficient quantities of protein is an essential prelude to a structure determination, but for many viral and human proteins this cannot be achieved using prokaryotic expression systems. Groups in the Structural Proteomics In Europe (SPINE) consortium have developed and implemented high-throughput (HTP) methodologies for cloning, expression screening and protein production in eukaryotic systems. Studies focused on three systems: yeast (Pichia pastoris and Saccharomyces cerevisiae), baculovirus-infected insect cells and transient expression in mammalian cells. Suitable vectors for HTP cloning are described and results from their use in expression screening and protein-production pipelines are reported. Strategies for co-expression, selenomethionine labelling (in all three eukaryotic systems) and control of glycosylation (for secreted proteins in mammalian cells) are assessed. © International Union of Crystallography, 2006.

Published
2006

7. Eukaryotic expression:Developments for structural proteomics

Author

Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Abstract

The production of sufficient quantities of protein is an essential prelude to a structure determination, but for many viral and human proteins this cannot be achieved using prokaryotic expression systems. Groups in the Structural Proteomics In Europe (SPINE) consortium have developed and implemented high-throughput (HTP) methodologies for cloning, expression screening and protein production in eukaryotic systems. Studies focused on three systems: yeast (Pichia pastoris and Saccharomyces cerevisiae), baculovirus-infected insect cells and transient expression in mammalian cells. Suitable vectors for HTP cloning are described and results from their use in expression screening and protein-production pipelines are reported. Strategies for co-expression, selenomethionine labelling (in all three eukaryotic systems) and control of glycosylation (for secreted proteins in mammalian cells) are assessed. © International Union of Crystallography, 2006.

Published
2006

8. Eukaryotic expression: developments for structural proteomics

Author

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Published
2006

9. Eukaryotic expression: developments for structural proteomics

Author

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Published
2006

10. Eukaryotic expression:Developments for structural proteomics

Author

Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Abstract

The production of sufficient quantities of protein is an essential prelude to a structure determination, but for many viral and human proteins this cannot be achieved using prokaryotic expression systems. Groups in the Structural Proteomics In Europe (SPINE) consortium have developed and implemented high-throughput (HTP) methodologies for cloning, expression screening and protein production in eukaryotic systems. Studies focused on three systems: yeast (Pichia pastoris and Saccharomyces cerevisiae), baculovirus-infected insect cells and transient expression in mammalian cells. Suitable vectors for HTP cloning are described and results from their use in expression screening and protein-production pipelines are reported. Strategies for co-expression, selenomethionine labelling (in all three eukaryotic systems) and control of glycosylation (for secreted proteins in mammalian cells) are assessed. © International Union of Crystallography, 2006.

Published
2006

11. Eukaryotic expression: developments for structural proteomics

Author

Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A. R., Assenberg, R., Bill, R. M., Busso, D., Chang, V. T., Davis, S. J., Dubrovsky, A., Gustafsson, L.L., Hedfalk, K., Heinemann, U., Jones, I. M., Ksiazek, D., Lang, Chim C, Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, Titia K, Sussman, Joel L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Published
2006

12. Eukaryotic expression:Developments for structural proteomics

Author

Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., Jones, E. Yvonne, Aricescu, A.R., Assenberg, R., Bill, Roslyn M., Busso, D., Chang, V.T., Davis, S.J., Dubrovsky, A., Gustafsson, L., Hedfalk, K., Heinemann, U., Jones, I.M., Ksiazek, D., Lang, C., Maskos, K., Messerschmidt, A., Macieira, S., Peleg, Y., Perrakis, A., Poterszman, A., Schneider, G., Sixma, T.K., Sussman, J.L., Sutton, G., Tarboureich, N., Zeev-Ben-Mordehai, T., and Jones, E. Yvonne

Abstract

The production of sufficient quantities of protein is an essential prelude to a structure determination, but for many viral and human proteins this cannot be achieved using prokaryotic expression systems. Groups in the Structural Proteomics In Europe (SPINE) consortium have developed and implemented high-throughput (HTP) methodologies for cloning, expression screening and protein production in eukaryotic systems. Studies focused on three systems: yeast (Pichia pastoris and Saccharomyces cerevisiae), baculovirus-infected insect cells and transient expression in mammalian cells. Suitable vectors for HTP cloning are described and results from their use in expression screening and protein-production pipelines are reported. Strategies for co-expression, selenomethionine labelling (in all three eukaryotic systems) and control of glycosylation (for secreted proteins in mammalian cells) are assessed. © International Union of Crystallography, 2006.

Published
2006

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