Conditional protein splicing via disulfide bond formation
نویسندگان
چکیده
منابع مشابه
Protein folding guides disulfide bond formation.
The Anfinsen principle that the protein sequence uniquely determines its structure is based on experiments on oxidative refolding of a protein with disulfide bonds. The problem of how protein folding drives disulfide bond formation is poorly understood. Here, we have solved this long-standing problem by creating a general method for implementing the chemistry of disulfide bond formation and rup...
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Storage of proteins is a physiological means to provide a reservoir for regulated utilization by the organism. Examples are the intracellular storage of exportable proteins in secretion granules, e.g., in exocrine glands, and the extracellular deposition of secretory proteins, e.g., of thyroglobulin (TG) in the lumina of thyroid follicles. In all cases, tight packaging of protein molecules is o...
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The majority of disulfide-linked cytosolic proteins are thought to be enzymes that transiently form disulfide bonds while catalyzing oxidation-reduction (redox) processes. Recent evidence indicates that reactive oxygen species can act as signaling molecules by promoting the formation of disulfide bonds within or between select redox-sensitive proteins. However, few studies have attempted to exa...
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Protein splicing is a post-translational modification in which an intein domain excises itself out of a host protein. Here, we investigate how the steps in the splicing process are coordinated so as to maximize the production of the final splice products and minimize the generation of undesired cleavage products. Our approach has been to prepare a branched intermediate (and analogs thereof) of ...
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ژورنال
عنوان ژورنال: The FASEB Journal
سال: 2013
ISSN: 0892-6638,1530-6860
DOI: 10.1096/fasebj.27.1_supplement.789.3