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The supercoiling motif is the most complex type of nontrivial topology found in proteins with at least one disulfide bond and, to the best of our knowledge, it has not been studied before. We show that a protein from extremophilic species with such a motif can fold; however, the supercoiling changes a smooth landscape observed in reduced conditions into a two-state folding process in the oxidative conditions, with a deep intermediate state. The protein takes advantage of the hairpinlike motif to overcome the topological barrier and thus to supercoil. We find that the depth of the supercoiling motif, i.e., the length of the threaded terminus, has a crucial impact on the folding rates of the studied protein. We show that fluctuations of the minimal surface area can be used to measure local stability, and we find that supercoiling introduces stability into the protein. We suggest that the supercoiling motif enables the studied protein to live in physically extreme conditions, which are detrimental to most life on Earth.
This article was published in the following journal.
Name: Physical review letters
Previously, we demonstrated that transcription-coupled DNA supercoiling (TCDS) potently activated or inhibited nearby promoters in Escherichia coli even in the presence of all four DNA topoisomerases,...
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Due to helical structure of DNA, massive amounts of positive supercoils are constantly introduced ahead of each replication fork. Positive supercoiling inhibits progression of replication forks but va...
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The ability of a protein to retain its structural conformation or its activity when subjected to physical or chemical manipulations.
A cytoskeletal linker protein with a molecular weight of greater than 500 kDa. It binds INTERMEDIATE FILAMENTS; MICROTUBULES; and MICROFILAMENTS and plays a central role in the organization and stability of the CYTOSKELETON. Plectin is phosphorylated by CALMODULIN KINASE; PROTEIN KINASE A; and PROTEIN KINASE C.
A pulmonary surfactant associated-protein that plays an essential role in alveolar stability by lowering the surface tension at the air-liquid interface. Inherited deficiency of pulmonary surfactant-associated protein B is one cause of RESPIRATORY DISTRESS SYNDROME, NEWBORN.
A pulmonary surfactant associated protein that plays a role in alveolar stability by lowering the surface tension at the air-liquid interface. It is a membrane-bound protein that constitutes 1-2% of the pulmonary surfactant mass. Pulmonary surfactant-associated protein C is one of the most hydrophobic peptides yet isolated and contains an alpha-helical domain with a central poly-valine segment that binds to phospholipid bilayers.
Sequences within RNA that regulate the processing, stability (RNA STABILITY) or translation (TRANSLATION, GENETIC) of RNA.
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