Protein folding in the bacterial periplasm.
نویسندگان
چکیده
منابع مشابه
Protein quality control in the bacterial periplasm
The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in Escherichia coli are initially synthesized in the cytoplasm, then follow a pathway that depends upon their ultimate cellular destination. Many proteins destined for the periplasm are synthesized as precursors carrying an N-terminal signal seq...
متن کاملFolding of a bacterial outer membrane protein during passage through the periplasm.
The transport of bacterial outer membrane proteins to their destination might be either a one-step process via the contact zones between the inner and outer membrane or a two-step process, implicating a periplasmic intermediate that inserts into the membrane. Furthermore, folding might precede insertion or vice versa. To address these questions, we have made use of the known 3D-structure of the...
متن کاملReview Protein quality control in the bacterial periplasm
The proper functioning of extracytoplasmic proteins requires their export to, and productive folding in, the correct cellular compartment. All proteins in Escherichia coli are initially synthesized in the cytoplasm, then follow a pathway that depends upon their ultimate cellular destination. Many proteins destined for the periplasm are synthesized as precursors carrying an N-terminal signal seq...
متن کاملA Stress Sensor for the Bacterial Periplasm
DegS, the periplasmic stress sensor, becomes activated when its PDZ domain recognizes the improperly exposed C-terminal sequences of outer membrane porins. This interaction relieves the inhibition of the neighboring protease domain of DegS, triggering a proteolysis cascade that leads to the sigma(E)-driven expression of periplasmic chaperones.
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ژورنال
عنوان ژورنال: Journal of bacteriology
سال: 1997
ISSN: 0021-9193
DOI: 10.1128/jb.179.8.2465-2471.1997