Rapid degradation of solid-phase bound peptides by the 20S proteasome


Proteasomes are cellular proteases involved in the degradation of numerous cellular proteins. The 20S proteasome is a cylindrical 28-mer protein complex composed of two outer heptameric α-rings forming the entrance for the protein substrate and two inner heptameric β-rings carrying the catalytic sites. Numerous in vitro studies have provided evidence that the 20S proteasome may degrade peptides of various lengths and even unfolded full-length polypeptide chains. However, a direct demonstration that the 20S proteasome may also cleave surface-attached immobilized peptides is lacking so far. To this end, we used a model system by coupling peptides from different source proteins covalently to the surface of glass beads and applied nanoLC/MS analysis to monitor the generation of proteolytic fragments in the presence of the 20S proteasome. Detectable amounts of cleavage products occurred within a few minutes indicating a much higher cleavage rate than observed with the same substrates in solution. Our finding lends support to the idea that proteasomes may directly degrade segments of membrane-bound proteins protruding into the aqueous phase. Copyright © 2013 European Peptide Society and John Wiley & Sons, Ltd.


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J. Pept. Sci.
J. Pept. Sci. 19(9): 588-97
28th Jul 2013

Marc Hovestädt, Ulrike Kuckelkorn, Agathe Niewienda, Christin Keller, Andrean Goede, Bernhard Ay, Stefan Günther, Katharina Janek, Rudolf Volkmer, Hermann-Georg Holzhütter

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[Hermann-Georg Holzhütter]

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  • Created: 9th Sep 2013 at 15:19
  • Last updated: 24th Oct 2013 at 16:14

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