The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence

scientific article

The cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence is …
instance of (P31):
scholarly articleQ13442814

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P356DOI10.1073/PNAS.85.10.3363
P932PMC publication ID280209
P698PubMed publication ID3285342
P5875ResearchGate publication ID19871651

P50authorGunnar von HeijneQ5619162
P2093author name stringDalbey RE
Wickner W
P2860cites workTrans-membrane Translocation of Proteins. The Direct Transfer ModelQ30409012
The distribution of positively charged residues in bacterial inner membrane proteins correlates with the trans-membrane topologyQ33880780
Three-dimensional structure of membrane and surface proteinsQ34258165
Intracellular protein topogenesisQ36360251
The Assembly of Proteins into Biological Membranes: The Membrane Trigger HypothesisQ38000320
Protein translocation across and integration into membranesQ39500270
Mechanism of incorporation of cell envelope proteins in Escherichia coliQ40248345
Import of honeybee prepromelittin into the endoplasmic reticulum: structural basis for independence of SRP and docking protein.Q41345662
The ;heavy' subunit of the photosynthetic reaction centre from Rhodopseudomonas viridis: isolation of the gene, nucleotide and amino acid sequenceQ41401089
Bacterial leader peptidase, a membrane protein without a leader peptide, uses the same export pathway as pre-secretory proteinsQ41564569
Analysis of the distribution of charged residues in the N-terminal region of signal sequences: implications for protein export in prokaryotic and eukaryotic cells.Q41581591
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
Bovine opsin has more than one signal sequenceQ49486981
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
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
Effects of the complete removal of basic amino acid residues from the signal peptide on secretion of lipoprotein in Escherichia coliQ70257285
Translocation of domains of nascent periplasmic proteins across the cytoplasmic membrane is independent of elongationQ70373251
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
P433issue10
P407language of work or nameEnglishQ1860
P921main subjectEscherichia coliQ25419
poisoningQ114953
P304page(s)3363-3366
P577publication date1988-05-01
P1433published inProceedings of the National Academy of Sciences of the United States of AmericaQ1146531
P1476titleThe cytoplasmic domain of Escherichia coli leader peptidase is a "translocation poison" sequence
P478volume85

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
Q57381643A signal peptide with a proline next to the cleavage site inhibits leader peptidase when present in a sec -independent protein
Q27666695Autotransporter passenger domain secretion requires a hydrophobic cavity at the extracellular entrance of the β-domain pore
Q40653179C-terminal sequences can inhibit the insertion of membrane proteins into the endoplasmic reticulum of Saccharomyces cerevisiae
Q36173436Conditionally lethal amber mutations in the leader peptidase gene of Escherichia coli
Q57381683Control of topology and mode of assembly of a polytopic membrane protein by positively charged residues
Q48077632De novo design of integral membrane proteins
Q54661918Different sec-requirements for signal peptide cleavage and protein translocation in a model E. coli protein.
Q37949470Export of the periplasmic maltose-binding protein of Escherichia coli
Q36253726Identification of a virB10 protein aggregate in the inner membrane of Agrobacterium tumefaciens
Q36216627In vitro insertion of leader peptidase into Escherichia coli membrane vesicles
Q37055727Insertion of proteins into bacterial membranes: mechanism, characteristics, and comparisons with the eucaryotic process
Q37039867Leader peptidase
Q33921342Mapping of catalytically important domains in Escherichia coli leader peptidase
Q36105138Membrane topology and mutational analysis of the TolQ protein of Escherichia coli required for the uptake of macromolecules and cell envelope integrity
Q50463977Molecular cloning of the Salmonella typhimurium lep gene in Escherichia coli
Q40343904Organization of dimethyl sulfoxide reductase in the plasma membrane of Escherichia coli.
Q33570175Positive charges in the cytoplasmic domain of Escherichia coli leader peptidase prevent an apolar domain from functioning as a signal
Q57381637Positively charged amino acids placed next to a signal sequence block protein translocation more efficiently in Escherichia coli than in mammalian microsomes
Q57381598Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane
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
Q41530383Signal peptidase I of Bacillus subtilis: patterns of conserved amino acids in prokaryotic and eukaryotic type I signal peptidases.
Q34227404Signal peptidases and signal peptide hydrolases
Q42126957Targeting of passenger protein domains to multiple intracellular membranes
Q44890199The 'positive-inside rule' applies to thylakoid membrane proteins
Q39454274The rational design of amino acid sequences by artificial neural networks and simulated molecular evolution: de novo design of an idealized leader peptidase cleavage site
Q37942677The signal peptide
Q40655505Topology and functional domains of Sec63p, an endoplasmic reticulum membrane protein required for secretory protein translocation
Q30369923Use of phoA fusions to study the topology of the Escherichia coli inner membrane protein leader peptidase

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