Chaperoning Anfinsen: the steric foldases

@article{Pauwels2007ChaperoningAT,
  title={Chaperoning Anfinsen: the steric foldases},
  author={Kristof Pauwels and Inge Van Molle and Jan Tommassen and Patrick van Gelder},
  journal={Molecular Microbiology},
  year={2007},
  volume={64}
}
Some proteins are so much resistant to proteolysis and unfolding that they violate folding rules shared by the vast majority of proteins. These unusual proteins manage to fold into an active native conformation that is thermodynamically at best marginally, but often even less stable than the unfolded state. A huge energetic barrier traps these proteins kinetically in the folded state. The drawback of this situation is the need for a specialized chaperone that adds steric information to the… Expand
The Chaperonopathies: Diseases with Defective Molecular Chaperones
In the mid 1950’s the Nobel Prize Laureate Christian B. Anfinsen from his research on the folding of ribonuclease A,1 began to concentrate on the problem of the relationship between structure andExpand
Decoding the Folding of Burkholderia glumae Lipase: Folding Intermediates En Route to Kinetic Stability
TLDR
It is demonstrated that the native lipase has a kinetically stable conformation and it is shown that a newly discovered molten globule-like conformation has distinct properties that clearly differ from those of the near-native intermediate state. Expand
Structural biology of periplasmic chaperones.
TLDR
This chapter aims to provide an overview of protein chaperones so far identified in the periplasm and how structural biology has assisted with the elucidation of their functions. Expand
The Membrane‐Integrated Steric Chaperone Lif Facilitates Active Site Opening of Pseudomonas aeruginosa Lipase A
TLDR
It is speculated that further interactions of PaLipA with the Xcp secretion machinery and/or components of the extracellular matrix contribute to the remaining activity of secreted PaLips, according to the computational and in vitro biochemical results. Expand
Modeling protein folding in vivo
TLDR
Computational modeling of protein folding should deemphasize the notion of unassisted thermodynamically controlled folding, and should focus instead on the step-by-step reverse engineering of the folding process as it actually occurs in vivo. Expand
Foldase and inhibitor functionalities of the pepsinogen prosegment are encoded within discrete segments of the 44 residue domain.
TLDR
The high sequence conservation of PS1-29 and its role in catalyzing pepsin folding strongly suggest that there is a conserved PS-catalyzed folding mechanism shared by pepin-like aspartic proteases with this motif. Expand
Studies of protein folding pathways
Protein folding is a problem of great importance in both the life sciences and biotechnology industries. This review begins with a brief summary of the physics of protein folding in vivo, which weExpand
Conserved Prosegment Residues Stabilize a Late-Stage Folding Transition State of Pepsin Independently of Ground States
TLDR
Results indicated that the prosegment, which is only 44 residues long, has evolved a high density of contacts that preferentially stabilize the folding transition state over the ground states, postulated that the poetrygment forms extensive non-native contacts during the process of catalyzing correct inter- and intra-domain contact during the final stages of folding. Expand
Structural Basis for Action of the External Chaperone for a Propeptide-deficient Serine Protease from Aeromonas sobria*
TLDR
It is revealed that operons encoding subtilases and their external chaperones are widely distributed among Gram-negative bacteria, suggesting that ASP and its homologs form a novel family of subtilase family having an external chapersone. Expand
Affinity-based isolation of a bacterial lipase through steric chaperone interactions.
TLDR
A new purification procedure of the lipase (LipA) that is endogenously secreted by the Gram-negative bacterium Burkholderia glumae is reported, which combines the specific binding scaffold of a lipase-specific foldase and the intrinsic resistance to chemical denaturation of LipA. Expand
...
1
2
3
4
...

References

SHOWING 1-10 OF 46 REFERENCES
Energetic landscape of α-lytic protease optimizes longevity through kinetic stability
During the evolution of proteins the pressure to optimize biological activity is moderated by a need for efficient folding. For most proteins, this is accomplished through spontaneous folding to aExpand
Protein memory through altered folding mediated by intramolecular chaperones
TLDR
The results indicate that an identical polypeptide can fold into an altered conformation through a mutated intramolecular chaperone and maintains memory of the folding process, which may be important in investigations of protein folding. Expand
Unfolded conformations of α-lytic protease are more stable than its native state
α-Lytic protease (αLP), an extracellular bacterial protease, is synthesized with a large amino-terminal pro-region that is essential for its folding in vivo and in vitro,. In the absence of theExpand
Role of the lipase-specific foldase of Burkholderia glumae as a steric chaperone.
TLDR
Results demonstrate that the Lif functions in a way analogous to the propeptides of many bacterial proteases and indicate that the amino acid sequence of the lipase does not contain all the information required for the protein to adopt its three-dimensional structure. Expand
Convergent evolution of clamp-like binding sites in diverse chaperones
Molecular chaperones have evolved diverse tertiary and quaternary structures to stabilize non-native polypeptides and facilitate their transition to the native state. Indeed, different families ofExpand
Comprehensive analysis of protein folding activation thermodynamics reveals a universal behavior violated by kinetically stable proteases.
TLDR
This work studies the temperature-dependences of the folding and unfolding kinetics of alpha LP and SGPB without their pro regions, and compares their behavior to a comprehensive set of other proteins to find some remarkable universal behaviors in the thermodynamically stable proteins. Expand
Folding of subtilisin BPN': characterization of a folding intermediate.
TLDR
A folding mechanism for subtilisin BPN' that comprises a high energy transition state, which is lowered by the interaction with the pro-sequence is supported, which supports the hypothesis that a common folding mechanism has been developed through convergent evolution. Expand
Structure of α-lytic protease complexed with its pro region
While the majority of proteins fold rapidly and spontaneously to their native states, the extracellular bacterial protease α-lytic protease (αLP) has a t1/2 for folding of ~2,000 years, correspondingExpand
Folding pathway mediated by an intramolecular chaperone: intrinsically unstructured propeptide modulates stochastic activation of subtilisin.
TLDR
The work on SbtE establishes that through selection of an intrinsically unstructured IMC domain, nature appears to have selected for a viable deterministic handle that controls a fundamentally random event of protease activation. Expand
Pilus chaperones represent a new type of protein-folding catalyst
TLDR
Periplasmic type 1 pilus chaperone FimC binds non-native pilus subunits and accelerates folding of the subunit FimG by 100-fold, and represents a previously unknown type of protein-folding catalyst and simultaneously acts as a kinetic trap preventing spontaneous subunit assembly in the periplasm. Expand
...
1
2
3
4
5
...