ArticleProceedings of the National Academy of Sciences of the United States of America2009
Cleavage of RseA by RseP requires a carboxyl-terminal hydrophobic amino acid following DegS cleavage.
Article in Proceedings of the National Academy of Sciences of the United States of America, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 37 papers.
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Who cites it
37 citing papers in PubMed.
- Article
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- Status of macromolecular crystallography beamlines at SSRF.Journal of synchrotron radiation · 2025Article
- Dual membrane-spanning anti-sigma factors regulate vesiculation inProceedings of the National Academy of Sciences of the United States of America · 2024Article
- In vivo characterization of the bacterial intramembrane-cleaving protease RseP using the heme binding tag-based assay iCliPSpy.Communications biology · 2023Article
- The role of site-2-proteases in bacteria: a review on physiology, virulence, and therapeutic potential.microLife · 2023Review
- Article
- PG1659 functions as anti-sigma factor to extracytoplasmic function sigma factor RpoE in Porphyromonas gingivalis W83.Molecular oral microbiology · 2021Article
- Involvement of a Membrane-Bound Amphiphilic Helix in Substrate Discrimination and Binding by anFrontiers in microbiology · 2020Article
- PDZ Domains Across the Microbial World: Molecular Link to the Proteases, Stress Response, and Protein Synthesis.Genome biology and evolution · 2019Article
- Maintaining Integrity Under Stress: Envelope Stress Response Regulation of Pathogenesis in Gram-Negative Bacteria.Frontiers in cellular and infection microbiology · 2019Review
- Evidence that regulation of intramembrane proteolysis is mediated by substrate gating during sporulation in Bacillus subtilis.PLoS genetics · 2018Article
- Role of extracytoplasmic function sigma factor PG1660 (RpoE) in the oxidative stress resistance regulatory network of Porphyromonas gingivalis.Molecular oral microbiology · 2018Article
- Bacillus subtilis Intramembrane Protease RasP Activity in Escherichia coli andJournal of bacteriology · 2017Article
- New Insights into the Regulation of Cell-Surface Signaling Activity Acquired from a Mutagenesis Screen of theFrontiers in microbiology · 2017Article
- Two stress sensor proteins for the expression of sigmaE regulon: DegS and RseB.Journal of microbiology (Seoul, Korea) · 2015Review
- Copper economy in Chlamydomonas: prioritized allocation and reallocation of copper to respiration vs. photosynthesis.Proceedings of the National Academy of Sciences of the United States of America · 2015Article
- A conserved activation cluster is required for allosteric communication in HtrA-family proteases.Structure (London, England : 1993) · 2015Article
- 1.15 Å resolution structure of the proteasome-assembly chaperone Nas2 PDZ domain.Acta crystallographica. Section F, Structural biology communications · 2014Article
- Proteolysis inside the membrane is a rate-governed reaction not driven by substrate affinity.Cell · 2013Article
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7 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Regulated intramembrane proteolysis (RIP) by the Site-2 protease (S2P) results in the release of a transmembrane signaling protein. Curiously, however, S2P cleavage must be preceded by the action of the Site-1 protease (S1P). To decipher the underlying mechanism, we reconstituted sequential, in vitro cleavages of the Escherichia coli transmembrane protein RseA by DegS (S1P) and RseP (S2P). After DegS cleavage, the newly exposed carboxyl-terminal residue Val-148 of RseA plays an essential role for RseP cleavage, and its mutation to charged or dissimilar amino acids crippled the Site-2 cleavage. By contrast, the identity of residues 146 and 147 of RseA has no impact on Site-2 cleavage. These results explain why Site-1 cleavage must precede Site-2 cleavage. Structural analysis reveals that the putative peptide-binding groove in the second, but not the first, PDZ domain of RseP is poised for binding to a single hydrophobic amino acid. These observations suggest that after DegS cleavage, the newly exposed carboxyl terminus of RseA may facilitate Site-2 cleavage through direct interaction with the PDZ domain.
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