Premium
MotE serves as a new chaperone specific for the periplasmic motility protein, MotC, in Sinorhizobium meliloti
Author(s) -
Eggenhofer Elke,
Haslbeck Martin,
Scharf Birgit
Publication year - 2004
Publication title -
molecular microbiology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.857
H-Index - 247
eISSN - 1365-2958
pISSN - 0950-382X
DOI - 10.1111/j.1365-2958.2004.04022.x
Subject(s) - periplasmic space , biology , chaperone (clinical) , sinorhizobium meliloti , microbiology and biotechnology , biochemistry , signal peptide , motility , biophysics , peptide sequence , mutant , gene , escherichia coli , medicine , pathology
Summary The flagella of Sinorhizobium meliloti rotate solely clockwise and vary their rotary speed to provoke changes in the swimming path. This mode of motility control has its molecular corollary in two novel motility proteins, MotC and MotD, present in addition to the ubiquitous MotA/MotB energizing proton channel. MotC binds to the periplasmic portion of MotB, whereas MotD interacts with FliM at the cytoplasmic face of the rotor. We report here the assignment and analysis of a fifth motility protein, MotE. Deletion of motE resulted in aggregation and decay of the periplasmic MotC protein and, as a consequence, in paralysis of the cell. The 179‐residue MotE protein bears an N‐terminal signal peptide and is rapidly secreted to the periplasm, where it forms stable dimers that are linked by a disulphide bridge between the cysteine 53 residues. Both, the monomeric and the dimeric MotE bind to MotC, and dimerization is essential for MotE stability in the periplasm. We conclude that MotE is a periplasmic chaperone specific for MotC being responsible for its proper folding and stability. We also propose that the MotE dimer serves as a shuttle to target MotC to its binding site at MotB.