Mapping polypeptide interactions of the SecA ATPase during translocation.
about
Protein translocation: what's the problem?Channel crossing: how are proteins shipped across the bacterial plasma membrane?Conformational Flexibility and Peptide Interaction of the Translocation ATPase SecAThe oligomeric state and arrangement of the active bacterial transloconDecatransin, a new natural product inhibiting protein translocation at the Sec61/SecYEG translocon.Conformational Changes of the Clamp of the Protein Translocation ATPase SecATwo copies of the SecY channel and acidic lipids are necessary to activate the SecA translocation ATPase.Position-dependent effects of polylysine on Sec protein transportMobility of the SecA 2-helix-finger is not essential for polypeptide translocation via the SecYEG complexStructural Similarities and Differences between Two Functionally Distinct SecA Proteins, Mycobacterium tuberculosis SecA1 and SecA2.Protein export by the mycobacterial SecA2 system is determined by the preprotein mature domain.Conserved SecA Signal Peptide-Binding Site Revealed by Engineered Protein Chimeras and Förster Resonance Energy Transfer.Defining the solution state dimer structure of Escherichia coli SecA using Förster resonance energy transferNew functions of the chloroplast Preprotein and Amino acid Transporter (PRAT) family members in protein import.SecA Cotranslationally Interacts with Nascent Substrate Proteins In Vivo.Characterization of the Escherichia coli SecA signal peptide-binding site.The dynamic action of SecA during the initiation of protein translocation.A "push and slide" mechanism allows sequence-insensitive translocation of secretory proteins by the SecA ATPase.Two-way communication between SecY and SecA suggests a Brownian ratchet mechanism for protein translocation.Preprotein mature domains contain translocase targeting signals that are essential for secretion.Direct identification of the site of binding on the chaperone SecB for the amino terminus of the translocon motor SecA.Ion conductivity of the bacterial translocation channel SecYEG engaged in translocation.The Sec System: Protein Export in Escherichia coli.Driving Forces of Translocation Through Bacterial Translocon SecYEG.The superoxide dismutase SodA is targeted to the periplasm in a SecA-dependent manner by a novel mechanism.The way is the goal: how SecA transports proteins across the cytoplasmic membrane in bacteria.
P2860
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P2860
Mapping polypeptide interactions of the SecA ATPase during translocation.
description
2009 nî lūn-bûn
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2009年の論文
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2009年学术文章
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name
Mapping polypeptide interactions of the SecA ATPase during translocation.
@en
Mapping polypeptide interactions of the SecA ATPase during translocation.
@nl
type
label
Mapping polypeptide interactions of the SecA ATPase during translocation.
@en
Mapping polypeptide interactions of the SecA ATPase during translocation.
@nl
prefLabel
Mapping polypeptide interactions of the SecA ATPase during translocation.
@en
Mapping polypeptide interactions of the SecA ATPase during translocation.
@nl
P2860
P356
P1476
Mapping polypeptide interactions of the SecA ATPase during translocation.
@en
P2093
Benedikt W Bauer
P2860
P304
20800-20805
P356
10.1073/PNAS.0910550106
P407
P50
P577
2009-11-20T00:00:00Z