ArticleBiochemical and biophysical research communications2014
The dispensability and requirement of SecA N-terminal aminoacyl residues for complementation, membrane binding, lipid-specific domains and channel activities.
Article in Biochemical and biophysical research communications, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 11 papers.
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Who cites it
11 citing papers in PubMed.
- Interaction of the motor protein SecA and the bacterial protein translocation channel SecYEG in the absence of ATP.Nanoscale advances · 2020Article
- SecA-Mediated Protein Translocation through the SecYEG Channel.Microbiology spectrum · 2019Review
- SecA inhibitors as potential antimicrobial agents: differential actions on SecA-only and SecA-SecYEG protein-conducting channels.FEMS microbiology letters · 2018Review
- Specific cardiolipin-SecY interactions are required for proton-motive force stimulation of protein secretion.Proceedings of the National Academy of Sciences of the United States of America · 2018Article
- Driving Forces of Translocation Through Bacterial Translocon SecYEG.The Journal of membrane biology · 2018Article
- An alternate mode of oligomerization for E. coli SecA.Scientific reports · 2017Article
- Article
- Using Chemical Probes to Assess the Feasibility of Targeting SecA for Developing Antimicrobial Agents against Gram-Negative Bacteria.ChemMedChem · 2016Article
- Lipids Activate SecA for High Affinity Binding to the SecYEG Complex.The Journal of biological chemistry · 2016Article
- The role and significance of potential lipid-binding regions in the mitochondrial protein import motor: an in-depth in silico study.3 Biotech · 2015Article
- Characterization of the minimal length of functional SecA in Escherichia coli.Biochemical and biophysical research communications · 2015Article
Corrections and comments
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Authors and funding
6 authors.
Funding
Abstract
SecA is an essential multifunctional protein for the translocation of proteins across bacterial membranes. Though SecA is known to function in the membrane, the detailed mechanism for this process remains unclear. In this study we constructed a series of SecA N-terminal deletions and identified two specific domains crucial for initial SecA/membrane interactions. The first small helix, the linker and part of the second helix (Δ2-22) were found to be dispensable for SecA activity in complementing the growth of a SecA ts mutant. However, deletions of N-terminal aminoacyl residues 23-25 resulted in severe progressive retardation of growth. Moreover, a decrease of SecA activity caused by N-terminal deletions correlated to the loss of SecA membrane binding, formation of lipid-specific domains and channel activity. All together, the results indicate that the N-terminal aminoacyl residues 23-25 play a critical role for SecA binding to membranes and that the N-terminal limit of SecA for activity is at the 25th amino acid.
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