ArticleMolecular microbiology2008
An amphiphilic region in the cytoplasmic domain of KdpD is recognized by the signal recognition particle and targeted to the Escherichia coli membrane.
Article in Molecular microbiology, 2008. 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, 21 citations in OpenAlex.
- The Dynamic SecYEG Translocon.Frontiers in molecular biosciences · 2021Review
- Two Signal Recognition Particle Sequences Are Present in the Amino-Terminal Domain of the C-Tailed Protein SciP.Journal of bacteriology · 2020Article
- Posttranslational insertion of small membrane proteins by the bacterial signal recognition particle.PLoS biology · 2020Article
- The SRP signal sequence of KdpD.Scientific reports · 2019Article
- Targeting and Insertion of Membrane Proteins.EcoSal Plus · 2017Review
- SecA drives transmembrane insertion of RodZ, an unusual single-span membrane protein.Journal of molecular biology · 2015Article
- Mechanisms of integral membrane protein insertion and folding.Journal of molecular biology · 2015Review
- Article
- Membrane interaction of the portal protein gp20 of bacteriophage T4.Journal of virology · 2012Article
- Biogenesis of bacterial inner-membrane proteins.Cellular and molecular life sciences : CMLS · 2010Review
- Protein localization in Escherichia coli cells: comparison of the cytoplasmic membrane proteins ProP, LacY, ProW, AqpZ, MscS, and MscL.Journal of bacteriology · 2010Article
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Authors and funding
6 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The sensor protein KdpD of Escherichia coli is composed of a large N-terminal hydrophilic region (aa 1-400), four transmembrane regions (aa 401-498) and a large hydrophilic region (aa 499-894) at the C-terminus. KdpD requires the signal recognition particle (SRP) for its targeting to the membrane. Deletions within KdpD show that the first 50 residues are required for SRP-driven membrane insertion. A fusion protein of the green fluorescent protein (GFP) with KdpD is found localized at the membrane only when SRP is present. The membrane targeting of GFP was not observed when the first 50 KdpD residues were deleted. A truncated mutant of KdpD containing only the first 25 amino acids fused to GFP lost its ability to specifically interact with SRP, whereas a specific interaction between SRP and the first 48 amino acids of KdpD fused to GFP was confirmed by pull-down experiments. Conclusively, a small amphiphilic region of 27 residues within the amino-terminal domain of KdpD (aa 22-48) is recognized by SRP and targets the protein to the membrane. This shows that membrane proteins with a large N-terminal region in the cytoplasm can be membrane-targeted early on to allow co-translational membrane insertion of their distant transmembrane regions.
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