Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal

scientific article

Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1002/J.1460-2075.1989.TB03618.X
P932PMC publication ID401099
P698PubMed publication ID2676512

P2093author name stringDalbey RE
R. E. Dalbey
J. K. Laws
Laws JK
P2860cites workConstruction of Biologically Functional Bacterial Plasmids In VitroQ24562887
The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequenceQ33573182
Alteration of the amino terminus of the mature sequence of a periplasmic protein can severely affect protein export in Escherichia coliQ33655946
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topologyQ33880780
Topogenic signals in integral membrane proteinsQ34167358
Determinants of membrane protein topologyQ34372343
Amphipathic analysis and possible formation of the ion channel in an acetylcholine receptorQ36245224
NH2-terminal hydrophobic region of influenza virus neuraminidase provides the signal function in translocationQ36256980
Intracellular protein topogenesisQ36360251
The Assembly of Proteins into Biological Membranes: The Membrane Trigger HypothesisQ38000320
Secretion and membrane localization of proteins in Escherichia coli.Q40285614
Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein.Q41345662
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteinsQ41564569
The transmembrane segment of the human transferrin receptor functions as a signal peptide.Q42571061
Primary structure and transmembrane orientation of the murine anion exchange proteinQ43489711
Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranesQ43822332
The internal signal sequence of Escherichia coli leader peptidase is necessary, but not sufficient, for its rapid membrane assemblyQ46238232
A small hydrophobic domain anchors leader peptidase to the cytoplasmic membrane of Escherichia coliQ48342898
High-level expression of M13 gene II protein from an inducible polycistronic messenger RNA.Q48382462
Sequence of the leader peptidase gene of Escherichia coli and the orientation of leader peptidase in the bacterial envelopeQ48395760
Leader peptidase catalyzes the release of exported proteins from the outer surface of the Escherichia coli plasma membrane.Q52457501
Leader peptidase of Escherichia coli: critical role of a small domain in membrane assembly.Q52493373
Multiple mechanisms of protein insertion into and across membranes.Q53779152
Role of amino-terminal positive charge on signal peptide in staphylokinase export across the cytoplasmic membrane of Escherichia coli.Q54764861
An artificial anchor domain: hydrophobicity suffices to stop transfer.Q54796961
An internal signal sequence: The asialoglycoprotein receptor membrane anchorQ56775313
Foreign transmembrane peptides replacing the internal signal sequence of transferrin receptor allow its translocation and membrane bindingQ57849730
The cytoplasmic carboxy terminus of M13 procoat is required for the membrane insertion of its central domainQ68891385
The role of the polar, carboxyl-terminal domain of Escherichia coli leader peptidase in its translocation across the plasma membraneQ68901815
Many random sequences functionally replace the secretion signal sequence of yeast invertaseQ68925585
Effects of two sec genes on protein assembly into the plasma membrane of Escherichia coliQ69881818
Introduction of basic amino acid residues after the signal peptide inhibits protein translocation across the cytoplasmic membrane of Escherichia coli. Relation to the orientation of membrane proteinsQ70229449
Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coliQ70257285
Synthesis, assembly into the cytoplasmic membrane, and proteolytic processing of the precursor of coliphage M13 coat proteinQ72125855
The isolation of homogeneous leader peptidase from a strain of Escherichia coli which overproduces the enzymeQ72932795
P433issue7
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
P304page(s)2095-2099
P577publication date1989-07-01
P1433published inThe EMBO JournalQ1278554
P1476titlePositive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal
P478volume8

Reverse relations

cites work (P2860)
Q37613694A 30-residue-long "export initiation domain" adjacent to the signal sequence is critical for protein translocation across the inner membrane of Escherichia coli
Q36685188Charge composition features of model single-span membrane proteins that determine selection of YidC and SecYEG translocase pathways in Escherichia coli
Q35930775Decoding signals for membrane protein assembly using alkaline phosphatase fusions
Q33921342Mapping of catalytically important domains in Escherichia coli leader peptidase
Q50463977Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli
Q57381637Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
Q36777551Proteolysis in protein import and export: Signal peptide processing in eu-and prokaryotes
Q34043693Sec dependent and sec independent assembly of E. coli inner membrane proteins: the topological rules depend on chain length
Q33334929Sequence and TnphoA analysis of a Mycoplasma hyorhinis protein with membrane export function
Q27691857The Sec translocase
Q29615298The complete general secretory pathway in gram-negative bacteria
Q37942677The signal peptide
Q40890215The topological analysis of integral cytoplasmic membrane proteins
Q37694639The translocation of negatively charged residues across the membrane is driven by the electrochemical potential: evidence for an electrophoresis-like membrane transfer mechanism
Q37636890Translocation of N-terminal tails across the plasma membrane
Q44417229Translocation of Phospholipids Is Facilitated by a Subset of Membrane-spanning Proteins of the Bacterial Cytoplasmic Membrane

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