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Article

Escherichia coli SecA truncated at its termini is functional and dimeric.

FEBS letters - 14 Feb 2005

Karamanou Spyridoula, Sianidis Giorgos, Gouridis Giorgos, Pozidis Charalambos, Papanikolau Yiannis, Papanikou Efrosyni, Economou Anastassios

Abstract excerpt

Terminal residues in SecA, the dimeric ATPase motor of bacterial preprotein translocase, were proposed to be required for function and dimerization. To test this, we generated truncation mutants of the 901aa long SecA of Escherichia coli. We now show that deletions of carboxy-terminal domain (CTD), the extreme CTD of 70 residues, or of the N-terminal nonapeptide or of both, do not compromise protein translocation...

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Identifiers

PMID: 15710424
DOI: 10.1016/j.febslet.2005.01.025

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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.

Related research

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Research trail→

Click a neighbor to travelStep 1 · 12 closest

Escherichia coli SecA truncated at its termini is functional and dimeric.PMID 15710424Read ↗

Reexamination of the role of the amino terminus of SecA in promoting its dimerization and functional state.Semantic proximity Read ↗

Characterization of the minimal length of functional SecA in Escherichia coli.Semantic proximity Read ↗

Roles of the C-terminal end of SecY in protein translocation and viability of Escherichia coli.Semantic proximity Read ↗

Identification of the preprotein binding domain of SecA.Semantic proximity Read ↗

Indecisive M13 procoat protein mutants bind to SecA but do not activate the translocation ATPase.Semantic proximity Read ↗

SecY and SecA interact to allow SecA insertion and protein translocation across the Escherichia coli plasma membrane.Semantic proximity Read ↗

Dimeric SecA is essential for protein translocation.Semantic proximity Read ↗

Residues essential for the function of SecE, a membrane component of the Escherichia coli secretion apparatus, are located in a conserved cytoplasmic region.Semantic proximity Read ↗

Arginine 357 of SecY is needed for SecA-dependent initiation of preprotein translocation.Semantic proximity Read ↗

Additional in vitro and in vivo evidence for SecA functioning as dimers in the membrane: dissociation into monomers is not essential for protein translocation in Escherichia coli.Semantic proximity Read ↗

Roles of the conserved cytoplasmic region and non-conserved carboxy-terminal region of SecE in Escherichia coli protein translocase.Semantic proximity Read ↗

Cross-linked SecA dimers are not functional in protein translocation.Semantic proximity Read ↗

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