Abstract：
:Biogenesis of the Gram-negative outer membrane involves the chaperone seventeen kilodalton protein (Skp). A Skp trimer is currently thought to bind its unfolded outer membrane protein (uOMP) substrates. Using sedimentation equilibrium, we discovered that Skp is not an obligate trimer under physiological conditions and that Na(+), Cl(-), Mg(2+), and PO4(3-) ions are not linked to Skp trimerization. These findings suggest that electrostatics play a negligible role in Skp assembly. Our results demonstrate that Skp monomers are populated at biologically relevant concentrations, which raises the idea that kinetic formation of Skp-uOMP complexes likely involves Skp monomer assembly around its substrate. In addition, van't Hoff analysis of Skp self-association does not support a previously proposed coupled folding and trimerization of Skp.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Sandlin CW,Zaccai NR,Fleming KGdoi
10.1021/acs.biochem.5b00806subject
Has Abstractpub_date
2015-12-08 00:00:00pages
7059-62issue
48eissn
0006-2960issn
1520-4995journal_volume
54pub_type
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