Membrane protein degradation by FtsH can be initiated from either end

Journal of Bacteriology

Volumn 184, Issue 17, 2002, Pages 4775-4782

  Chiba, Shinobu ^a   Akiyama, Yoshinori ^a   Ito, Koreaki ^a  

^a KYOTO UNIVERSITY   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; METALLOPROTEINASE; PROTEIN FTSH; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CATALYSIS; ESCHERICHIA COLI; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ALKALINE PHOSPHATASE; AMINO ACID SEQUENCE; ATP-DEPENDENT PROTEASES; BACTERIAL PROTEINS; CYCLIN-DEPENDENT KINASES; CYTOPLASM; CYTOSOL; ESCHERICHIA COLI PROTEINS; MEMBRANE PROTEINS; MOLECULAR SEQUENCE DATA;

ESCHERICHIA COLI; NEGIBACTERIA;

EID: 0036720126     PISSN: 00219193     EISSN: None     Source Type: Journal    
DOI: 10.1128/JB.184.17.4775-4782.2002     Document Type: Article

References (45)

1. Chloroplast protease: Possible regulators of gene expression?
2. Topology analysis of the SecY protein, an integral membrane protein involved in protein export in Escherichia coli
3. Roles of multimerization and membrane association in the proteolytic functions of FtsH (HflB)
4. Subunit a of proton ATPase F0 sector is a substrate of the FtsH protease in Escherichia coli
5. FtsH (HflB) is an ATP-dependent protease selectively acting on SecY and some other membrane proteins
6. FtsH, a membrane-bound ATPase, forms a complex in the cytoplasmic membrane of Escherichia coli
7. FtsH recognizes proteins with unfolded structure and hydrolyzes the carboxyl side of hydrophobic residues
8. Crystal structure of heat shock locus V (HslV) from Escherichia coli
9. Length recognition at the N-terminal tail of membrane proteins as a mode of initiation of FtsH-mediated proteolysis
10. Interposon mutagenesis of soil and water bacteria: A family of DNA fragments designed for in vitro insertional mutagenesis of gram-negative bacteria
11. Recognition, targeting, and hydrolysis of the λ O replication protein by the ClpP/ClpX protease
12. Regulation by proteolysis: Developmental switches
13. The ClpXP and ClpAP proteases degrade proteins with carboxy-terminal peptide tails added by the SsrA-tagging system
14. Structure of 20S proteasome from yeast at 2.4 Ä resolution
15. Degradation of carboxy-terminal-tagged cytoplasmic protein by the Escherichia coli protease HflB (FtsH)
16. Substrate recognition by the ClpA chaperone component of ClpAP protease
17. Translocation pathway of protein substrates in ClpAP protease
18. FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit
19. A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY
20. Differential pathways for protein degradation by the FtsH/HflKC membrane-embedded protease complex: An implication from the interference by a mutant form of a new substrate protein, YccA
21. Dislocation of membrane proteins in FtsH-mediated proteolysis
22. AAA proteases: Cellular machines for degrading membrane proteins
23. ATP-dependent proteases degrade their substrates by processively unraveling them from the degradation signal
24. Membrane protein degradation by AAA proteases in mitochondria: Extraction of substrates from either membrane surface
25. Crystal structure of the 20S proteasome from the archaeon T. acidophilum
26. Syd, a SecY-interacting protein, excludes SecA from the SecYE complex with an altered SecY24 subunit
27. AAA+: A class of chaperone-like ATPases associated with the assembly, operation, and disassembly of protein complexes
28. SecY is an indispensable component of the protein secretory machinery of Escherichia coli
29. AAA+ superfamily ATPase: Common structure-diverse function
30. Balanced biosynthesis of major membrane components through regulated degradation of the committed enzyme of lipid A biosynthesis by the AAA protease FtsH (HflB) in Escherichia coli
31. Visualization of substrate binding and translocation by the ATP-dependent protease, ClpXP
32. The AAA term: Related ATPases with diverse functions
33. ClpA mediates directional translocation of substrate proteins into the ClpP protease
34. Directed evolution of green fluorescent protein by a new versatile PCR strategy for site-directed and semi-random mutagenesis
35. The secE gene encodes an integral membrane protein required for protein export in Escherichia coli
36. Structure and mechanism of ATP-dependent protease
37. Proteolysis of bacteriophage λ CII by Escherichia coli FtsH (HflB)
38. Additions and corrections to differential in vivo roles played by DsbA and DsbC in the formation of protein disulfide bonds
39. Determinants of the quantity of the stable SecY complex in the Escherichia coli cell
40. Topology and subcellular localization of FtsH protein in Escherichia coli
41. AAA proteins: Lords of ring
42. The structure of ClpP at 2.3 Å resolution suggests a model for ATP-dependent proteolysis
43. An efficient recombination system for chromosome engineering in Escherichia coli