FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W134020194> ?p ?o ?g. }

• W134020194 endingPage "220" @default.
• W134020194 startingPage "207" @default.
• W134020194 abstract "A signal peptide is required for the entry of a protein into the secretory pathway but how it functions in concert with the other transport components to achieve protein localization is not known. In Escherichia coli, SecA is a component of the transport machinery which may play a role in targeting the preprotein to membrane-bound translocation sites and then utilize the energy of ATP hydrolysis to initiate membrane insertion of the preprotein. This model requires that the signal peptide interact specifically with SecA and that features of the signal peptide promote binding. These issues were examined using a wild type synthetic signal sequence derived from E. coli alkaline phosphatase and several model signal peptides that differ in amino-terminal charge, core region hydrophobicity, and the ability to form an α-helical structure. Using a SecA/lipid ATPase assay as an indicator of binding, we observe maximum activity with the functional wild type peptide, 3K7L and 1K7L; these have very hydrophobic core regions and a high propensity for α-helix formation, while no significant reactions were noted for the non-functional peptides, 3K2L and 1K2L. Although peptides of intermediate hydrophobicity, 3K4L and 1K4L, both stimulated the SecA ATPase activity to an intermediate extent, the level of stimulation was more marked with the 3K4L peptide. This is consistent with in vivo analyses which indicate that for signal peptides of intermediate hydrophobicity, the amino terminal basic residues also play a key role in enhancing transport activity. The data suggest that signal peptide core region hydrophobicity, amino-terminal charge, and α-helicity contribute to the modulation of SecA/lipid ATPase activity by altering the binding affinity of the peptide for SecA. Separately, a competition binding assay was employed to establish that signal peptides also interact with SecA in aqueous solution. Furthermore, the interaction of functional signal peptides with SecA alters the SecA conformation sufficiently, for both soluble and membrane-associated forms, to cause a marked change in its V8 protease sensitivity." @default.
• W134020194 created "2016-06-24" @default.
• W134020194 creator A5020544332 @default.
• W134020194 creator A5030447237 @default.
• W134020194 creator A5051111957 @default.
• W134020194 date "2005-12-06" @default.
• W134020194 modified "2023-09-25" @default.
• W134020194 title "Model Signal Peptides: Probes of Molecular Interactions During Protein Secretion" @default.
• W134020194 cites W1480251791 @default.
• W134020194 cites W1488637794 @default.
• W134020194 cites W1511994212 @default.
• W134020194 cites W1515069540 @default.
• W134020194 cites W1542734815 @default.
• W134020194 cites W1548395234 @default.
• W134020194 cites W1557193358 @default.
• W134020194 cites W1567962789 @default.
• W134020194 cites W1572793754 @default.
• W134020194 cites W1587914816 @default.
• W134020194 cites W1602373369 @default.
• W134020194 cites W1605434051 @default.
• W134020194 cites W1666626663 @default.
• W134020194 cites W1679608726 @default.
• W134020194 cites W171398818 @default.
• W134020194 cites W1964169934 @default.
• W134020194 cites W1976221987 @default.
• W134020194 cites W1979080606 @default.
• W134020194 cites W1979839256 @default.
• W134020194 cites W1980750447 @default.
• W134020194 cites W1992470956 @default.
• W134020194 cites W2000489621 @default.
• W134020194 cites W2002707099 @default.
• W134020194 cites W2005356879 @default.
• W134020194 cites W2005966867 @default.
• W134020194 cites W2008415333 @default.
• W134020194 cites W2011869957 @default.
• W134020194 cites W2012811483 @default.
• W134020194 cites W2022703044 @default.
• W134020194 cites W2022855757 @default.
• W134020194 cites W2030128644 @default.
• W134020194 cites W2040338718 @default.
• W134020194 cites W2048052250 @default.
• W134020194 cites W2060249357 @default.
• W134020194 cites W2066537459 @default.
• W134020194 cites W2073075045 @default.
• W134020194 cites W2084407726 @default.
• W134020194 cites W2086597706 @default.
• W134020194 cites W2094729609 @default.
• W134020194 cites W2095056890 @default.
• W134020194 cites W2100837269 @default.
• W134020194 cites W2127755216 @default.
• W134020194 cites W2143197682 @default.
• W134020194 cites W2203768638 @default.
• W134020194 cites W247603372 @default.
• W134020194 doi "https://doi.org/10.1007/0-306-46890-5_15" @default.
• W134020194 hasPublicationYear "2005" @default.
• W134020194 type Work @default.
• W134020194 sameAs 134020194 @default.
• W134020194 citedByCount "0" @default.
• W134020194 crossrefType "book-chapter" @default.
• W134020194 hasAuthorship W134020194A5020544332 @default.
• W134020194 hasAuthorship W134020194A5030447237 @default.
• W134020194 hasAuthorship W134020194A5051111957 @default.
• W134020194 hasConcept C104317684 @default.
• W134020194 hasConcept C10858879 @default.
• W134020194 hasConcept C115335371 @default.
• W134020194 hasConcept C12554922 @default.
• W134020194 hasConcept C141315368 @default.
• W134020194 hasConcept C144647389 @default.
• W134020194 hasConcept C156399914 @default.
• W134020194 hasConcept C167625842 @default.
• W134020194 hasConcept C181199279 @default.
• W134020194 hasConcept C185592680 @default.
• W134020194 hasConcept C23265538 @default.
• W134020194 hasConcept C2779281246 @default.
• W134020194 hasConcept C41625074 @default.
• W134020194 hasConcept C49039625 @default.
• W134020194 hasConcept C515207424 @default.
• W134020194 hasConcept C55493867 @default.
• W134020194 hasConcept C57581600 @default.
• W134020194 hasConcept C86803240 @default.
• W134020194 hasConceptScore W134020194C104317684 @default.
• W134020194 hasConceptScore W134020194C10858879 @default.
• W134020194 hasConceptScore W134020194C115335371 @default.
• W134020194 hasConceptScore W134020194C12554922 @default.
• W134020194 hasConceptScore W134020194C141315368 @default.
• W134020194 hasConceptScore W134020194C144647389 @default.
• W134020194 hasConceptScore W134020194C156399914 @default.
• W134020194 hasConceptScore W134020194C167625842 @default.
• W134020194 hasConceptScore W134020194C181199279 @default.
• W134020194 hasConceptScore W134020194C185592680 @default.
• W134020194 hasConceptScore W134020194C23265538 @default.
• W134020194 hasConceptScore W134020194C2779281246 @default.
• W134020194 hasConceptScore W134020194C41625074 @default.
• W134020194 hasConceptScore W134020194C49039625 @default.
• W134020194 hasConceptScore W134020194C515207424 @default.
• W134020194 hasConceptScore W134020194C55493867 @default.
• W134020194 hasConceptScore W134020194C57581600 @default.
• W134020194 hasConceptScore W134020194C86803240 @default.

• next