منابع مشابه
Multitasking SecB chaperones in bacteria
Protein export in bacteria is facilitated by the canonical SecB chaperone, which binds to unfolded precursor proteins, maintains them in a translocation competent state and specifically cooperates with the translocase motor SecA to ensure their proper targeting to the Sec translocon at the cytoplasmic membrane. Besides its key contribution to the Sec pathway, SecB chaperone tasking is critical ...
متن کاملDirected evolution of SecB chaperones toward toxin-antitoxin systems.
SecB chaperones assist protein export in bacteria. However, certain SecB family members have diverged to become specialized toward the control of toxin-antitoxin (TA) systems known to promote bacterial adaptation to stress and persistence. In such tripartite TA-chaperone (TAC) systems, the chaperone was shown to assist folding and to prevent degradation of its cognate antitoxin, thus facilitati...
متن کاملProtein folding: Who chaperones nascent chains in bacteria?
Important advances in biology often occur when problems that have been controversial and seemingly complex are resolved with surprisingly simple and clear answers. Such has been the case with the problem of how proteins fold inside cells, which has seen a number of controversies and solutions in the past decade. A very recent example of this concerns the physiological functions of two molecular...
متن کاملCatalysis of protein folding by chaperones in pathogenic bacteria.
Molecular chaperones are thought to inhibit off-pathway interactions such as aggregation from occurring without influencing the on-pathway formation of native structure. Here, we present a mechanism whereby the family of PapD-like chaperones, which are involved in the formation of adhesive pili in pathogenic bacteria, function by suppressing aggregation while simultaneously catalyzing the foldi...
متن کاملLon protease quality control of presecretory proteins in Escherichia coli and its dependence on the SecB and DnaJ (Hsp40) chaperones.
Various environmental insults result in irreversible damage to proteins and protein complexes. To cope, cells have evolved dedicated protein quality control mechanisms involving molecular chaperones and proteases. Here, we provide both genetic and biochemical evidence that the Lon protease and the SecB and DnaJ/Hsp40 chaperones are involved in the quality control of presecretory proteins in Esc...
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ژورنال
عنوان ژورنال: Frontiers in Microbiology
سال: 2014
ISSN: 1664-302X
DOI: 10.3389/fmicb.2014.00666