SecB is a bona fide generalized chaperone in Escherichia coli
نویسندگان
چکیده
منابع مشابه
SecB is a bona fide generalized chaperone in Escherichia coli.
It is known that the DnaK and Trigger Factor (TF) chaperones cooperate in the folding of newly synthesized cytosolic proteins in Escherichia coli. We recently showed that despite a very narrow temperature range of growth and high levels of aggregated cytosolic proteins, E. coli can tolerate deletion of both chaperones, suggesting that other chaperones might be involved in this process. Here, we...
متن کاملP. falciparum cpn20 Is a Bona Fide Co-Chaperonin That Can Replace GroES in E. coli
Human malaria is among the most ubiquitous and destructive tropical, parasitic diseases in the world today. The causative agent, Plasmodium falciparum, contains an unusual, essential organelle known as the apicoplast. Inhibition of this degenerate chloroplast results in second generation death of the parasite and is the mechanism by which antibiotics function in treating malaria. In order to be...
متن کاملCARMIL is a bona fide capping protein interactant.
CARMIL, also known as Acan 125, is a multidomain protein that was originally identified on the basis of its interaction with the Src homology 3 (SH3) domain of type I myosins from Acanthamoeba. In a subsequent study of CARMIL from Dictyostelium, pull-down assays indicated that the protein also bound capping protein and the Arp2/3 complex. Here we present biochemical evidence that Acanthamoeba C...
متن کاملChaperone SecB from Escherichia coli mediates kinetic partitioning via a dynamic equilibrium with its ligands.
We have shown that the complexes between SecB, a chaperone from Escherichia coli, and two physiological ligands, galactose-binding protein and maltose-binding protein, are in rapid, dynamic equilibrium between the bound and free states. Binding to SecB is readily reversible, and each time the ligand is released it undergoes a kinetic partitioning between folding to its native state and re-bindi...
متن کاملMouse Bestrophin-2 Is a Bona fide Cl− Channel
Bestrophins have recently been proposed to comprise a new family of Cl(-) channels. Our goal was to test whether mouse bestrophin-2 (mBest2) is a bona fide Cl(-) channel. We expressed mBest2 in three different mammalian cell lines. mBest2 was trafficked to the plasma membrane as shown by biotinylation and immunoprecipitation, and induced a Ca(2+)-activated Cl(-) current in all three cell lines ...
متن کاملذخیره در منابع من
با ذخیره ی این منبع در منابع من، دسترسی به آن را برای استفاده های بعدی آسان تر کنید
ژورنال
عنوان ژورنال: Proceedings of the National Academy of Sciences
سال: 2004
ISSN: 0027-8424,1091-6490
DOI: 10.1073/pnas.0402398101