SecB, a molecular chaperone with two faces
نویسندگان
چکیده
منابع مشابه
Unfolding thermodynamics of the tetrameric chaperone, SecB.
SecB is a cytosolic tetrameric chaperone in Escherichia coli, which maintains polypeptides, destined for export in a translocation competent state. The thermodynamics of unfolding of SecB was studied as a function of protein concentration, by using high sensitivity-differential scanning calorimetry and spectroscopic methods. The thermal unfolding of tetrameric SecB is reversible and can be well...
متن کاملSecB 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 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 کاملA thermodynamic coupling mechanism for the disaggregation of a model peptide substrate by chaperone secB.
Molecular chaperones prevent protein aggregation in vivo and in vitro. In a few cases, multichaperone systems are capable of dissociating aggregated state(s) of substrate proteins, although little is known of the mechanism of the process. SecB is a cytosolic chaperone, which forms part of the precursor protein translocation machinery in Escherichia coli. We have investigated the interaction of ...
متن کاملThe molecular chaperone SecB is released from the carboxy-terminus of SecA during initiation of precursor protein translocation.
The chaperone SecB keeps precursor proteins in a translocation-competent state and targets them to SecA at the translocation sites in the cytoplasmic membrane of Escherichia coli. SecA is thought to recognize SecB via its carboxy-terminus. To determine the minimal requirement for a SecB-binding site, fusion proteins were created between glutathione-S-transferase and different parts of the carbo...
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ژورنال
عنوان ژورنال: Trends in Microbiology
سال: 2001
ISSN: 0966-842X
DOI: 10.1016/s0966-842x(01)01980-1