Survey of large protein complexes in D. vulgaris reveals great structural diversity Export

@article{citeulike:6012157, abstract = {10.1073/pnas.0813068106 An unbiased survey has been made of the stable, most abundant multi-protein complexes in Hildenborough (H) that are larger than Mr \^{a}‰ˆ 400 k. The quaternary structures for 8 of the 16 complexes purified during this work were determined by single-particle reconstruction of negatively stained specimens, a success rate \^{a}‰ˆ10 times greater than that of previous \^{a}€œproteomic\^{a}€ screens. In addition, the subunit compositions and stoichiometries of the remaining complexes were determined by biochemical methods. Our data show that the structures of only two of these large complexes, out of the 13 in this set that have recognizable functions, can be modeled with confidence based on the structures of known homologs. These results indicate that there is significantly greater variability in the way that homologous prokaryotic macromolecular complexes are assembled than has generally been appreciated. As a consequence, we suggest that relying solely on previously determined quaternary structures for homologous proteins may not be sufficient to properly understand their role in another cell of interest.}, author = {Han, Bong-Gyoon and Dong, Ming and Liu, Haichuan and Camp, Lauren and Geller, Jil and Singer, Mary and Hazen, Terry C. and Choi, Megan and Witkowska, H. Ewa and Ball, David A. and Typke, Dieter and Downing, Kenneth H. and Shatsky, Maxim and Brenner, Steven E. and Chandonia, John-Marc and Biggin, Mark D. and Glaeser, Robert M.}, citeulike-article-id = {6012157}, citeulike-linkout-0 = {http://dx.doi.org/10.1073/pnas.0813068106}, citeulike-linkout-1 = {http://www.pnas.org/content/106/39/16580.abstract}, citeulike-linkout-2 = {http://www.pnas.org/content/106/39/16580.full.pdf}, citeulike-linkout-3 = {http://view.ncbi.nlm.nih.gov/pubmed/19805340}, citeulike-linkout-4 = {http://www.hubmed.org/display.cgi?uids=19805340}, day = {29}, doi = {10.1073/pnas.0813068106}, journal = {Proceedings of the National Academy of Sciences}, keywords = {complexes, drosophila, evolution, protein-protein-interactions, structures}, month = {September}, number = {39}, pages = {16580--16585}, posted-at = {2009-10-26 18:22:41}, priority = {2}, title = {Survey of large protein complexes in D. vulgaris reveals great structural diversity}, url = {http://dx.doi.org/10.1073/pnas.0813068106}, volume = {106}, year = {2009} }

TY - JOUR ID - citeulike:6012157 L3 - citeulike-article-id:6012157 N2 - 10.1073/pnas.0813068106 An unbiased survey has been made of the stable, most abundant multi-protein complexes in Hildenborough (H) that are larger than Mr ≈ 400 k. The quaternary structures for 8 of the 16 complexes purified during this work were determined by single-particle reconstruction of negatively stained specimens, a success rate ≈10 times greater than that of previous “proteomic” screens. In addition, the subunit compositions and stoichiometries of the remaining complexes were determined by biochemical methods. Our data show that the structures of only two of these large complexes, out of the 13 in this set that have recognizable functions, can be modeled with confidence based on the structures of known homologs. These results indicate that there is significantly greater variability in the way that homologous prokaryotic macromolecular complexes are assembled than has generally been appreciated. As a consequence, we suggest that relying solely on previously determined quaternary structures for homologous proteins may not be sufficient to properly understand their role in another cell of interest. IS - 39 JF - Proceedings of the National Academy of Sciences EP - 16585 TI - Survey of large protein complexes in D. vulgaris reveals great structural diversity VL - 106 SP - 16580 KW - complexes KW - drosophila KW - evolution KW - protein-protein-interactions KW - structures AU - Han, Bong-Gyoon AU - Dong, Ming AU - Liu, Haichuan AU - Camp, Lauren AU - Geller, Jil AU - Singer, Mary AU - Hazen, Terry AU - Choi, Megan AU - Witkowska, Ewa AU - Ball, David AU - Typke, Dieter AU - Downing, Kenneth AU - Shatsky, Maxim AU - Brenner, Steven AU - Chandonia, John-Marc AU - Biggin, Mark AU - Glaeser, Robert PY - 2009/09/29/ UR - http://dx.doi.org/10.1073/pnas.0813068106 ER -