ArticleProceedings of the National Academy of Sciences of the United States of America1997
The NG domain of the prokaryotic signal recognition particle receptor, FtsY, is fully functional when fused to an unrelated integral membrane polypeptide.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.
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Who cites it
31 citing papers in PubMed.
- Article
- Diversity in robustness of Lactococcus lactis strains during heat stress, oxidative stress, and spray drying stress.Applied and environmental microbiology · 2014Article
- Genetic evidence for functional interaction of the Escherichia coli signal recognition particle receptor with acidic lipids in vivo.The Journal of biological chemistry · 2010Article
- Archaea signal recognition particle shows the way.Archaea (Vancouver, B.C.) · 2010Review
- Article
- Article
- Protein transport across and into cell membranes in bacteria and archaea.Cellular and molecular life sciences : CMLS · 2010Review
- Predominant membrane localization is an essential feature of the bacterial signal recognition particle receptor.BMC biology · 2009Article
- The distinct anchoring mechanism of FtsY from different microbes.Current microbiology · 2009Article
- The membrane-binding motif of the chloroplast signal recognition particle receptor (cpFtsY) regulates GTPase activity.The Journal of biological chemistry · 2009Article
- Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli.Amino acids · 2008Review
- FtsY affects sporulation and antibiotic production by whiH in Streptomyces coelicolor.Current microbiology · 2008Article
- Conformational changes in the GTPase modules of the signal reception particle and its receptor drive initiation of protein translocation.The Journal of cell biology · 2007Article
- X-ray structures of the signal recognition particle receptor reveal targeting cycle intermediates.PloS one · 2007Article
- X-ray structure of the T. aquaticus FtsY:GDP complex suggests functional roles for the C-terminal helix of the SRP GTPases.Proteins · 2007Article
- Membrane binding of the bacterial signal recognition particle receptor involves two distinct binding sites.The Journal of cell biology · 2006Article
- Streptococcal viability and diminished stress tolerance in mutants lacking the signal recognition particle pathway or YidC2.Proceedings of the National Academy of Sciences of the United States of America · 2005Article
- The core Escherichia coli signal recognition particle receptor contains only the N and G domains of FtsY.Journal of bacteriology · 2004Article
- Structure and function of the chloroplast signal recognition particle.Current genetics · 2004Review
- Crystallization of the GMPPCP complex of the NG domains of Thermus aquaticus Ffh and FtsY.Acta crystallographica. Section D, Biological crystallography · 2003Article
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Authors and funding
4 authors.
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No grant is acknowledged in the PubMed record.
Abstract
Recent studies have revealed that Escherichia coli possesses an essential targeting system for integral membrane proteins, similar to the mammalian signal recognition particle (SRP) machinery. One essential protein in this system is FtsY, a homologue of the alpha-subunit of the mammalian SRP-receptor (SR-alpha). However, E. coli does not possess a close homologue of the integral membrane protein SR-beta, which anchors SR-alpha to the membrane. Moreover, although FtsY can be found as a peripheral membrane protein, the majority is found soluble in the cytoplasm. In this study, we obtained genetic and biochemical evidence that FtsY must be targeted to the membrane for proper function. We demonstrate that the essential membrane targeting activity of FtsY is mediated by a 198-residue-long acidic N-terminal domain. This domain can be functionally replaced by unrelated integral membrane polypeptides, thus avoiding the need for specific FtsY membrane targeting factors. Therefore, the N terminus of FtsY constitutes an independent domain, which is required only for the targeting of the C-terminal NG domain of FtsY to the membrane.
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