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Article

Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane.

FEBS letters - 27 Jun 1994

Andersson H, von Heijne G

Abstract excerpt

The sec machinery catalyzes the translocation of nascent polypeptide chains across the inner membrane of E. coli, yet some inner membrane proteins depend only weakly or not at all on an intact sec function for membrane insertion even though they have stretches of chain protruding into the periplasmic space. Earlier work has demonstrated that the length of a periplasmic loop correlates with its degree of...

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Identifiers

PMID: 8033997
DOI: 10.1016/0014-5793(94)00530-3

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Positively charged residues influence the degree of SecA dependence in protein translocation across the E. coli inner membrane.PMID 8033997Read ↗

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Importance of transmembrane segments in Escherichia coli SecY.Semantic proximity Read ↗

Fine-tuning the topology of a polytopic membrane protein: role of positively and negatively charged amino acids.Semantic proximity Read ↗

Escherichia coli SecA truncated at its termini is functional and dimeric.Semantic proximity Read ↗

The hydrophobic core of the Sec61 translocon defines the hydrophobicity threshold for membrane integration.Semantic proximity Read ↗

Polarity and charge of the periplasmic loop determine the YidC and sec translocase requirement for the M13 procoat lep protein.Semantic proximity Read ↗

Cardiolipin is required in vivo for the stability of bacterial translocon and optimal membrane protein translocation and insertion.Semantic proximity Read ↗

A gating motif in the translocation channel sets the hydrophobicity threshold for signal sequence function.Semantic proximity Read ↗

Dynamic action of the Sec machinery during initiation, protein translocation and termination.Semantic proximity Read ↗

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