ArticleThe EMBO journal1999
Dislocation of membrane proteins in FtsH-mediated proteolysis.
Article in The EMBO journal, 1999. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Who cites it
30 citing papers in PubMed, 112 citations in OpenAlex.
- Membrane-embedded polar residues target membrane proteins for degradation by the quality control protease FtsH.Nature communications · 2026Article
- FTSH PROTEASE 3 facilitates Complex I degradation through a direct interaction with the Complex I subunit PSST.The Plant cell · 2023Article
- Applications of Bacterial Degrons and Degraders - Toward Targeted Protein Degradation in Bacteria.Frontiers in molecular biosciences · 2021Review
- Integrated Proteomic and Transcriptomic Analyses Reveal the Roles ofFrontiers in microbiology · 2021Article
- Bacterial rhomboid proteases mediate quality control of orphan membrane proteins.The EMBO journal · 2020Article
- Proteolysis mediated by the membrane-integrated ATP-dependent protease FtsH has a unique nonlinear dependence on ATP hydrolysis rates.Protein science : a publication of the Protein Society · 2019Article
- Folding-Degradation Relationship of a Membrane Protein Mediated by the Universally Conserved ATP-Dependent Protease FtsH.Journal of the American Chemical Society · 2018Article
- Molecular insights into theThe Journal of biological chemistry · 2017Article
- Rewiring of the FtsH regulatory network by a single nucleotide change in saeS of Staphylococcus aureus.Scientific reports · 2017Article
- Membrane proteases in the bacterial protein secretion and quality control pathway.Microbiology and molecular biology reviews : MMBR · 2012Review
- Co-evolution of multipartite interactions between an extended tmRNA tag and a robust Lon protease in Mycoplasma.Molecular microbiology · 2009Article
- ATP-dependent proteases differ substantially in their ability to unfold globular proteins.The Journal of biological chemistry · 2009Article
- Characterization of the Cpx regulon in Escherichia coli strain MC4100.Journal of bacteriology · 2009Article
- Article
- Specific binding of D1 protein degradation products to the psbAI promoter in Synechococcus sp. strain PCC 7942.Journal of bacteriology · 2007Article
- The thylakoid lumen protease Deg1 is involved in the repair of photosystem II from photoinhibition in Arabidopsis.The Plant cell · 2007Article
- m-AAA protease-driven membrane dislocation allows intramembrane cleavage by rhomboid in mitochondria.The EMBO journal · 2007Article
- Shuttling mechanism of peroxisome targeting signal type 1 receptor Pex5: ATP-independent import and ATP-dependent export.Molecular and cellular biology · 2005Article
- Membrane protein turnover by the m-AAA protease in mitochondria depends on the transmembrane domains of its subunits.EMBO reports · 2004Article
- ATP-binding sites in brain p97/VCP (valosin-containing protein), a multifunctional AAA ATPase.The Biochemical journal · 2003Article
Corrections and comments
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Authors and funding
3 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Escherichia coli FtsH degrades several integral membrane proteins, including YccA, having seven transmembrane segments, a cytosolic N-terminus and a periplasmic C-terminus. Evidence indicates that FtsH initiates proteolysis at the N-terminal cytosolic domain. SecY, having 10 transmembrane segments, is also a substrate of FtsH. We studied whether and how the FtsH-catalyzed proteolysis on the cytosolic side continues into the transmembrane and periplasmic regions using chimeric proteins, YccA-(P3)-PhoA-His6-Myc and SecY-(P5)-PhoA, with the alkaline phosphatase (PhoA) mature sequence in a periplasmic domain. The PhoA domain that was present within the fusion protein was rapidly degraded by FtsH when it lacked the DsbA-dependent folding. In contrast, both PhoA itself and the TM9-PhoA region of SecY-(P5)-PhoA were stable when expressed as independent polypeptides. In the presence of DsbA, the FtsH-dependent degradation stopped at a site near to the N-terminus of the PhoA moiety, leaving the PhoA domain (and its C-terminal region) undigested. The efficiency of this degradation stop correlated well with the rapidity of the folding of the PhoA domain. Thus, both transmembrane and periplasmic domains are degraded by the processive proteolysis by FtsH, provided they are not tightly folded. We propose that FtsH dislocates the extracytoplasmic domain of a substrate, probably using its ATPase activity.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.