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Protein folding and degradation in bacteria:¶To degrade or not to degrade? That is the question
Cellular and Molecular Life Sciences, 2002In Escherichia coli protein quality control is carried out by a protein network, comprising chaperones and proteases. Central to this network are two protein families, the AAA+ and the Hsp70 family. The major Hsp70 chaperone. DnaK, efficiently prevents protein aggregation and supports the refolding of damaged proteins. In a special case, DnaK, together
Dougan, David A. +2 more
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Lysosomes and protein degradation
Biochemical Society Transactions, 1977Considerable evidence from studies with group-specific proteinase inhibitors, in particular pepstatin, the aspartic proteinase inhibitor, implicates lysosomes in turnover of endogenous cellular proteins. Recent experiments using a new group-specific inhibitor of thiol (cysteine) proteinases, Z-Phe-Ala-diazomethyl ketone, are described.
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Protein degradation in signaling
Current Opinion in Plant Biology, 2000Recent studies have linked proteolysis by the ubiquitin/proteasome pathway to a variety of signaling pathways in higher plants. These links were uncovered by characterization of mutants altered in signaling or by targeted disruption of components of the proteolytic pathway. Significant advances have recently revealed connections between proteolysis and
J, Callis, R D, Vierstra
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Experimental Gerontology, 2005
Continuous turnover of intracellular proteins is essential for the maintenance of cellular homeostasis and for the regulation of multiple cellular functions. The first reports showing a decrease in total rates of protein degradation with age are dated more than 50 years ago, when the major players in protein degradation where still to be discovered ...
Marta, Martinez-Vicente +2 more
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Continuous turnover of intracellular proteins is essential for the maintenance of cellular homeostasis and for the regulation of multiple cellular functions. The first reports showing a decrease in total rates of protein degradation with age are dated more than 50 years ago, when the major players in protein degradation where still to be discovered ...
Marta, Martinez-Vicente +2 more
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Archives of Biochemistry and Biophysics, 1953
Abstract Rate equations for a degrading system based on a simple step mechanism are considered. The initial attack is assumed to occur at random. It is followed by a further random depolymerization of the intermediate fragments but, in general, at a different rate.
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Abstract Rate equations for a degrading system based on a simple step mechanism are considered. The initial attack is assumed to occur at random. It is followed by a further random depolymerization of the intermediate fragments but, in general, at a different rate.
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Current Opinion in Chemical Biology, 2005
The ubiquitin-proteasome pathway plays a major role in cellular protein destruction and regulates fundamental cellular processes such as the cell cycle, cell signaling, and development. By altering the substrate recognition of ubiquitin-protein ligases, their robust proteolytic activity can be re-directed to recruit and accelerate the degradation of ...
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The ubiquitin-proteasome pathway plays a major role in cellular protein destruction and regulates fundamental cellular processes such as the cell cycle, cell signaling, and development. By altering the substrate recognition of ubiquitin-protein ligases, their robust proteolytic activity can be re-directed to recruit and accelerate the degradation of ...
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Ubiquitination and Degradation of Proteins
2011Modification by ubiquitin (Ub) and ubiquitin-like proteins (UbLs) is involved in the regulation of numerous cellular processes and has therefore become an important subject of research in various areas of biomedicine. The large number of components of the system (∼1,500), most of them being ligases (∼800) that recognize their target substrates ...
Yelena, Kravtsova-Ivantsiv +1 more
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Trends in Biochemical Sciences, 2005
1 Rheinberger, H-J. (2004) A history of protein biosynthesis andribosome research. In Protein Synthesis and Ribosome Structure(Nierhaus, K.H. and Wilson, D.N., eds), pp. 1–51, Wiley-VCH Verlag2 Green, A.A. et al. (1954) The structure of haemoglobin. IV. Signdetermination by the isomorphous replacement method. Proc. Roy.Soc. A225, 287–3073 Ban, N. et al.
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1 Rheinberger, H-J. (2004) A history of protein biosynthesis andribosome research. In Protein Synthesis and Ribosome Structure(Nierhaus, K.H. and Wilson, D.N., eds), pp. 1–51, Wiley-VCH Verlag2 Green, A.A. et al. (1954) The structure of haemoglobin. IV. Signdetermination by the isomorphous replacement method. Proc. Roy.Soc. A225, 287–3073 Ban, N. et al.
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Linkers for protein degradation
Nature Chemical Biology, 2018The ability to subvert E3 ubiquitin ligases with small-molecule drugs offers tremendous promise for drug discovery. A new study demonstrates how structural and computational techniques can engineer and exploit unnatural protein–protein interfaces to design selective protein degraders.
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Protein degradation in bacteria
Archives of Biochemistry and Biophysics, 1953Summary 1. Under aerobic conditions which permit growth of Escherichia coli , the rate of protein degradation, as measured by loss of labeled arginine from the acid-insoluble fraction of the culture, is at least 8 ± 2% per 30 hr. 2. When such cells grown in a synthetic medium are transferred to a secondary medium containing a complete amino ...
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