Structure and function of the molecular chaperone Trigger Factor
نویسندگان
چکیده
منابع مشابه
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Nerve growth factor (NGF) is a neurotrophic factor that is functional in the survival, maintenance and differentiation of nervous system cells. This protein has three subunits, of which the beta subunit has the main activity. Its structure consists of a cysteine knot motif made up of beta strands linked by disulfide bonds. It can be used as a therapeutic agent in the treatment of many diseases....
متن کاملChaperone and antichaperone activities of trigger factor.
Reduced denatured lysozyme tends to aggregate at neutral pH and competition between productive folding and aggregation substantially reduces the efficiency of refolding. Trigger factor, a folding catalyst and chaperone can, depending on the concentration of trigger factor and the solution conditions, cause either a substantial increase (chaperone activity) or a substantial decrease (antichapero...
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The molecular chaperone Hsp104 plays a central role in the clearance of aggregates after heat shock and the propagation of yeast prions. Hsp104's disaggregation activity and prion propagation have been linked to its ability to resolubilize or remodel protein aggregates. However, Hsp104 has also the capacity to catalyze protein aggregation of some substrates at specific conditions. Hence, it is ...
متن کاملEffect of C-terminal truncation on the molecular chaperone function and dimerization of Escherichia coli trigger factor.
To examine the role of the C-terminal domain in the chaperone function of trigger factor (TF), a number of truncation mutants were constructed, namely: TF419, TF389, TF380, TF360, TF344, and TF251, in which the C-terminal 13, 43, 52, 72, 88 residues or the entire C-domain were deleted, respectively. Co-expression of mutant chicken adenylate kinase (AK) with TF and the C-terminal truncation muta...
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ژورنال
عنوان ژورنال: Biochimica et Biophysica Acta (BBA) - Molecular Cell Research
سال: 2010
ISSN: 0167-4889
DOI: 10.1016/j.bbamcr.2010.01.017