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pro vyhledávání: '"R E, Dalbey"'
Publikováno v:
Methods in enzymology. 584
Signal peptidases are membrane proteases that play crucial roles in the protein transport pathway of bacteria. They cleave off the signal peptide from precursor proteins that are membrane inserted by the SecYEG or Tat translocons. Signal peptide clea
Autor:
R E, Dalbey
Publikováno v:
Molecular Microbiology. 5:2855-2860
The Escherichia coli leader peptidase has been vital for unravelling problems in membrane assembly and protein export. The role of this essential peptidase is to remove amino-terminal leader peptides from exported proteins after they have crossed the
Publikováno v:
The Journal of biological chemistry. 276(37)
The membrane insertion of the Sec-independent M13 Procoat protein in bacteria requires the membrane electrochemical potential and the integral membrane protein YidC. We show here that YidC is involved in the translocation but not in the targeting of
Publikováno v:
Pharmacologytherapeutics. 87(1)
Type I signal peptidases are essential membrane-bound serine proteases that function to cleave the amino-terminal signal peptide extension from proteins that are translocated across biological membranes. The bacterial signal peptidases are unique ser
Publikováno v:
Protein science : a publication of the Protein Society. 6(6)
The discovery that proteins exported from the cytoplasm are typically synthesized as larger precursors with cleavable signal peptides has focused interest on the peptidases that remove the signal peptides. Here, we review the membrane-bound peptidase
Publikováno v:
Journal of molecular biology. 245(4)
An effective method for the determination of the activity of signal peptidase I (SPase I) of Escherichia coli is established using the hybrid protein pro-OmpA-nuclease A as substrate. Pro-OmpA-nuclease A, a hybrid secretory precursor was purified to
Publikováno v:
The Journal of biological chemistry. 269(43)
We have studied the membrane insertion of two proteins from the inner membrane of Escherichia coli, both with two transmembrane segments connected by a short periplasmic loop: the M13 procoat protein and a mutant "inverted" leader peptidase. Neither
Autor:
W R, Tschantz, R E, Dalbey
Publikováno v:
Methods in enzymology. 244
Publikováno v:
The Journal of biological chemistry. 268(36)
We report that a thiol leader peptidase, produced by replacing the critical serine at position 90 with a cysteine residue, is enzymatically active. In contrast to the wild-type leader peptidase, the thiol enzyme can be inactivated with N-ethylmaleimi
Autor:
M, Sung, R E, Dalbey
Publikováno v:
The Journal of biological chemistry. 267(19)
Leader peptidase of Escherichia coli cleaves the leader sequence from the amino terminus of membrane and secreted proteins after these proteins insert across the membrane. Despite considerable research, the mechanism of catalysis of leader peptidase