The TolQ-TolR proteins energize TolA and share homologies with the flagellar motor proteins MotA-MotB
نویسندگان
چکیده
منابع مشابه
Co-overproduction and localization of the Escherichia coli motility proteins motA and motB.
The motility genes motA and motB of Escherichia coli were placed under control of the Serratia marcescens trp promoter. After induction with beta-indoleacrylic acid, the levels of MotA and MotB rose over about a 3-h period, reaching plateau levels approximately 50-fold higher than wild-type levels. Both overproduced proteins inserted into the cytoplasmic membrane. Growth and motility were essen...
متن کاملEnergy-dependent conformational change in the TolA protein of Escherichia coli involves its N-terminal domain, TolQ, and TolR.
TolQ, TolR, and TolA inner membrane proteins of Escherichia coli are involved in maintaining the stability of the outer membrane. They share homology with the ExbB, ExbD, and TonB proteins, respectively. The last is involved in energy transduction between the inner and the outer membrane, and its conformation has been shown to depend on the presence of the proton motive force (PMF), ExbB, and E...
متن کاملRole of TolR N-terminal, central, and C-terminal domains in dimerization and interaction with TolA and tolQ.
The Tol-PAL system of Escherichia coli is a multiprotein system involved in maintaining the cell envelope integrity and is necessary for the import of some colicins and phage DNA into the bacterium. It is organized into two complexes, one near the outer membrane between TolB and PAL and one in the cytoplasmic membrane between TolA, TolQ, and TolR. In the cytoplasmic membrane, all of the Tol pro...
متن کاملConformational change in the stator of the bacterial flagellar motor.
MotA and MotB are integral membrane proteins of Escherichia coli that form the stator of the proton-fueled flagellar rotary motor. The motor contains several MotA/MotB complexes, which function independently to conduct protons across the cytoplasmic membrane and couple proton flow to rotation. MotB contains a conserved aspartic acid residue, Asp32, that is critical for rotation. We have propose...
متن کاملAssembly of motor proteins, PomA and PomB, in the Na+-driven stator of the flagellar motor.
PomA and PomB are transmembrane proteins that form the stator complex in the sodium-driven flagellar motor of Vibrio alginolyticus and are believed to surround the rotor part of the flagellar motor. We constructed and observed green fluorescent protein (GFP) fusions of the stator proteins PomA and PomB in living cells to clarify how stator proteins are assembled and installed into the flagellar...
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ژورنال
عنوان ژورنال: Molecular Microbiology
سال: 2008
ISSN: 0950-382X,1365-2958
DOI: 10.1046/j.1365-2958.2001.02673.x