Abstract:
:An unbiased survey has been made of the stable, most abundant multi-protein complexes in Desulfovibrio vulgaris Hildenborough (DvH) that are larger than Mr approximately 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 approximately 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.
journal_name
Proc Natl Acad Sci U S Aauthors
Han BG,Dong M,Liu H,Camp L,Geller J,Singer M,Hazen TC,Choi M,Witkowska HE,Ball DA,Typke D,Downing KH,Shatsky M,Brenner SE,Chandonia JM,Biggin MD,Glaeser RMdoi
10.1073/pnas.0813068106subject
Has Abstractpub_date
2009-09-29 00:00:00pages
16580-5issue
39eissn
0027-8424issn
1091-6490pii
0813068106journal_volume
106pub_type
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