SecA insertion into phospholipids is stimulated by negatively charged lipids and inhibited by ATP: a monolayer study.

No abstract is available for this paper.

• Publication year

  1992

• Venue

  Biochemistry

• Publication date

  1992-02-04

• Fields of study

  Biology, Medicine, Chemistry

• Identifiers
  DOI 10.1021/BI00119A021PMID 1531180
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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• The ATPase activity of SecA is regulated by acidic phospholipids, SecY, and the leader and mature domains of precursor proteins.

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• Lipid involvement in protein translocation in Escherichia coli

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• Azide-resistant mutants of Escherichia coli alter the SecA protein, an azide-sensitive component of the protein export machinery.

  1990cited by this paper
• Complementation of two overlapping fragments of SecA, a protein translocation ATPase of Escherichia coli, allows ATP binding to its amino-terminal region.

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  1989cited by this paper
• The secE gene encodes an integral membrane protein required for protein export in Escherichia coli.

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• SecA protein, a peripheral protein of the Escherichia coli plasma membrane, is essential for the functional binding and translocation of proOmpA.

  1989cited by this paper
• SecA protein hydrolyzes ATP and is an essential component of the protein translocation ATPase of Escherichia coli.

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• Phosphatidylglycerol is involved in protein translocation across Escherichia coli inner membranes

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• Binding of SecA ATPase monomers and dimers to lipid vesicles.

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• Two distinct anionic phospholipid-dependent events involved in SecA-mediated protein translocation.

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• ESCHERICHIA COLI PREPROTEIN TRANSLOCASE Precursor protein translocation across the Escherichia coli inner membrane is mediated by the translocase which is composed of a heterotrimeric integral membrane protein complex with SecY, SecE, and SecG as subunits, and peripherally bound SecA. Cross-linking

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• Substrate Proteins Take Shape at an Improved Bacterial Translocon

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• Structural Elucidation of SecA Substrate and SecYEG Bound States Utilizing SecA-Preprotein Chimeras and Fluorescence Spectroscopy

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