Regulated Proteolysis in Microorganisms by Eyal Gur, Ralf Ottofueling, David A. Dougan (auth.), David

By Eyal Gur, Ralf Ottofueling, David A. Dougan (auth.), David A. Dougan (eds.)

This booklet includes an intensive selection of serious reports, from best researchers within the box of regulated protein degradation. It covers the position of regulated proteolysis in various microorganisms (from Gram confident, Gram unfavorable and pathogenic micro organism to Archaea and the Baker’s yeast Saccharomyces cerevisiae).

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18 E. Gur et al. The ClpA recognition motif within N-end rule substrates is a dihydrophobic element, located between five and nine residues from the primary destabilising residue at the N-terminus of the protein [74, 105]. Interestingly, one of the N-end rule substrates, Dps (DNA protection during starvation), which protects DNA from reactive oxygen species, contains two N-terminal recognition motifs. One motif is created after endoproteolytic cleavage of the first five residues of Dps, to generate Dps6–167 and is required for recognition by ClpS and ClpA [78, 79], the other N-terminal motif is created following cleavage of the N-terminal Met by methionine aminopeptidase (MetAP), to generate Dps2–167 which contains a ClpX (Nmotif-1) within the first five residues of Dps [96].

Sequence of clpA and identification of a Clp-specific substrate. J Biol Chem 265(14):7886–7893 101. Maglica Z, Striebel F, Weber-Ban E (2008) An intrinsic degradation tag on the ClpA C-terminus regulates the balance of ClpAP complexes with different substrate specificity. J Mol Biol 384(2):503–511 102. Hoskins JR, Singh SK, Maurizi MR, Wickner S (2000) Protein binding and unfolding by the chaperone ClpA and degradation by the protease ClpAP. Proc Natl Acad Sci U S A 97(16):8892–8897 103. Hoskins JR, Wickner S (2006) Two peptide sequences can function cooperatively to facilitate binding and unfolding by ClpA and degradation by ClpAP.

Interestingly, the various degradation motifs appear to be recognised by different regions within the unfoldase. g. g. e. SsrA-tagged substrates) do not require this domain for direct recognition [50, 52, 69]. For example, lO (a replication protein of bacteriophage l) carries an N-terminal degradation motif (N-motif 1, NH2-TNTAKI), which is specifically recognised by the N-terminal domain of ClpX [52, 96, 99]. Indeed deletion of this domain (from ClpX) inhibits the ClpP-mediated degradation of lO [52], which is proposed to result from the low affinity of this class of substrate to the axial loops on ClpX.

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