A protease complex in the Escherichia coli plasma membrane: HflKC (HflA) forms a complex with FtsH (HflB), regulating its proteolytic activity against SecY.
It is indicated that the proteolytic activity of FtsH is modulated negatively by its association with HflKC, and the possibility that even the wild‐type Hfl KC protein acts to antagonize FTSH is raised.
Secretion monitor, SecM, undergoes self-translation arrest in the cytosol.
Respiratory chain is required to maintain oxidized states of the DsbA-DsbB disulfide bond formation system in aerobically growing Escherichia coli cells.
- T. Kobayashi, S. Kishigami, M. Sone, H. Inokuchi, T. Mogi, K. Ito
- Biology, ChemistryProceedings of the National Academy of Sciences…
- 28 October 1997
Results suggest that the respiratory electron transfer chain participates in the oxidation of DsbA, by acting primarily on DsbB, and it is remarkable that a cellular catalyst of protein folding is connected to the respiratory chain.
FtsH is required for proteolytic elimination of uncomplexed forms of SecY, an essential protein translocase subunit.
Overproduction of SecY in the ftsH mutant cells proved to deleteriously affect cell growth and protein export, suggesting that elimination of uncomplexed SecY is important for optimum protein translocation and for the integrity of the membrane.
SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.
Data show that the SecA protein has a central role in coupling the hydrolysis of ATP to the transfer of pre‐secretory proteins across the membrane.
Mutation of Trp1254 in the multispecific organic anion transporter, multidrug resistance protein 2 (MRP2) (ABCC2), alters substrate specificity and results in loss of methotrexate transport activity.
- K. Ito, C. Oleschuk, C. Westlake, M. Vasa, R. Deeley, S. Cole
- BiologyThe Journal of biological chemistry
- 12 October 2001
The results demonstrate that Trp1254 plays an important role in the ability of MRP2 to transport conjugated organic anions and identify this amino acid in the putative last transmembrane segment (TM17) of this ABC protein as being critical for transport of MTX.
The Sec protein-translocation pathway.
Crystal structure of cobalt-containing nitrile hydratase.
- A. Miyanaga, S. Fushinobu, K. Ito, T. Wakagi
- ChemistryBiochemical and Biophysical Research…
- 16 November 2001
The crystal structure of cobalt-containing nitrile hydratase from Pseudonocardia thermophila JCM 3095 at 1.8 A resolution revealed the structure of the noncorrin cobalt at the catalytic center. Two…
Host regulation of lysogenic decision in bacteriophage lambda: transmembrane modulation of FtsH (HflB), the cII degrading protease, by HflKC (HflA).
It is proposed that this transmembrane modulation differentiates the FtsH actions to different substrate proteins such as the membrane-bound SecY protein and the cytosolic cII protein as part of the host control over lambda lysogenic decision.
Characterization of cold-sensitive secY mutants of Escherichia coli
The rapid temperature response in vivo and the impaired in vitro translocation activity at low temperatures with the secY39 mutant support the notion that SecY, a membrane-embedded secretion factor, participates in protein translocation across the bacterial cytoplasmic membrane.