rseP Antibody

1. we describe several methods for characterization of the proteolytic functions and structure of RseP mainly in vivo, including a proteolytic activity assay using model substrates, an in vitro analysis of cleavage of signal peptides in a detergent solution and in the membrane vesicles, structural analysis of membrane-embedded RseP based on the thiol modifiability of introduced cysteine residues, and the protein interaction PMID: 28065260
2. Mutations disturbing the possible beta-strand conformation of the loop impaired RseP proteolytic activity and that some of these mutations resulted in the differential cleavage of different substrates. PMID: 26447507
3. study concludes that recognition of the cleaved amino acid by the RseP PDZ domain is not essential for sequential cleavage of RseA and sigma(E) stress response in vivo PMID: 23016873
4. Escherichia coli RseP, an site-2 protease (S2P) family I-CLiP, introduces a cleavage into signal peptides after their signal peptidase-mediated liberation from preproteins PMID: 21810987
5. RseP, which is required for normal sigmaE activation, prevents toxicity due to the presence of two specific outer membrane proteins that are down-regulated by RseX PMID: 16513633
6. RseP catalyzes proteolytic cleavage of the membrane-bound anti-sigma(E) protein RseA as an essential step in transmembrane signal transduction in the sigma(E) extracytoplasmic stress response pathway. PMID: 18268014
7. circularly permutated PDZ domains control RseP, the S2P family intramembrane protease of Escherichia coli PMID: 18945679
8. after DegS cleavage, the newly exposed carboxyl terminus of RseA may facilitate Site-2 cleavage through direct interaction with the PDZ domain. PMID: 19706448

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KEGG: ecj:JW0171

STRING: 316385.ECDH10B_0156