Demonstration of a folded monomeric form of porin PhoE of Escherichia coli in vivo.
The porins in the outer membranes of gram-negative bacteria are trimeric proteins. A folded monomeric form of the Escherichia coli porin PhoE, with a higher electrophoretic mobility than that of the denatured protein, has recently been detected in in vitro folding studies. To investigate the possible biological significance of the folded monomer, we attempted to detect this form in vivo. After pulse-labeling, folded monomers could be detected by immunoprecipitation. Furthermore, folded monomers were detected in a preparation of mutant PhoE porins, in which the subunit interactions were weakened by a E-66-->R substitution. Together, these results show that the folded monomer is not an in vitro folding artifact but an integral part of the native trimer.
Van Gelder
P
P
Department of Molecular Cell Biology and Institute of Biomembranes, Utrecht University, The Netherlands.
Tommassen
J
J
D016521:Electrophoresis, Gel, Pulsed-Field; D004926:Escherichia coli / Q000378:metabolism*; D029968:Escherichia coli Proteins; D018272:Porins / Q000737:chemistry* / Q000378:metabolism; D017510:Protein Folding; D011993:Recombinant Fusion Proteins / Q000378:metabolism
D029968:Escherichia coli Proteins; D018272:Porins; D011993:Recombinant Fusion Proteins; C082922:PhoE protein, E coli