Localization of Functional Polypeptides in Bacterial Inclusion Bodies
نویسندگان
چکیده
منابع مشابه
Localization of functional polypeptides in bacterial inclusion bodies.
Bacterial inclusion bodies, while showing intriguing amyloid-like features, such as a beta-sheet-based intermolecular organization, binding to amyloid-tropic dyes, and origin in a sequence-selective deposition process, hold an important amount of native-like secondary structure and significant amounts of functional polypeptides. The aggregation mechanics supporting the occurrence of both misfol...
متن کاملLocalization of chaperones DnaK and GroEL in bacterial inclusion bodies.
By immunostaining and transmission electron microscopy, chaperones DnaK and GroEL have been identified at the solvent-exposed surface of bacterial inclusion bodies and entrapped within these aggregates, respectively. Functional implications of this distinct localization are discussed in the context of Escherichia coli protein quality control.
متن کاملConstruction and deconstruction of bacterial inclusion bodies.
Bacterial inclusion bodies (IBs) are refractile aggregates of protease-resistant misfolded protein that often occur in recombinant bacteria upon gratuitous overexpression of cloned genes. In biotechnology, the formation of IBs represents a main obstacle for protein production since even favouring high protein yields, the in vitro recovery of functional protein from insoluble deposits depends on...
متن کاملIsolation of cell-free bacterial inclusion bodies
BACKGROUND Bacterial inclusion bodies are submicron protein clusters usually found in recombinant bacteria that have been traditionally considered as undesirable products from protein production processes. However, being fully biocompatible, they have been recently characterized as nanoparticulate inert materials useful as scaffolds for tissue engineering, with potentially wider applicability i...
متن کاملBacterial Inclusion Bodies Contain Amyloid-Like Structure
Protein aggregation is a process in which identical proteins self-associate into imperfectly ordered macroscopic entities. Such aggregates are generally classified as amorphous, lacking any long-range order, or highly ordered fibrils. Protein fibrils can be composed of native globular molecules, such as the hemoglobin molecules in sickle-cell fibrils, or can be reorganized beta-sheet-rich aggre...
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ژورنال
عنوان ژورنال: Applied and Environmental Microbiology
سال: 2007
ISSN: 0099-2240,1098-5336
DOI: 10.1128/aem.01952-06