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Literature summary for 7.4.2.5 extracted from

  • Floyd, J.H.; You, Z.; Hsieh, Y.H.; Ma, Y.; Yang, H.; Tai, P.C.
    The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities (2014), Biochem. Biophys. Res. Commun., 453, 138-142.
    View publication on PubMedView publication on EuropePMC
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Protein Variants

Protein Variants Comment Organism
additional information construction of SecA N-terminal deletion mutants. The first small helix, the linker and part of the second helix (residues 2-22) are dispensable for SecA activity in complementing the growth of a SecA temperature-sensitive mutant. Deletions of N-terminal aminoacyl residues 23-25 result in severe progressive retardation of growth. A decrease of SecA activity caused by N-terminal deletions correlates to the loss of SecA membrane binding, formation of lipid-specific domains and channel activity. The N-terminal aminoacyl residues 23-25 play a critical role for SecA binding to membranes and the N-terminal limit of SecA for activity is at the 25th amino acid Escherichia coli

Organism

Organism UniProt Comment Textmining
Escherichia coli
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