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

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.

authors

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 RM

doi

10.1073/pnas.0813068106

subject

Has Abstract

pub_date

2009-09-29 00:00:00

pages

16580-5

issue

39

eissn

0027-8424

issn

1091-6490

pii

0813068106

journal_volume

106

pub_type

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