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The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization
by
Li, Yongquan
, Shen, Xueling
, Mao, Xuming
, Li, Shanzhen
, Du, Yiling
in
Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Binding
/ Biological and medical sciences
/ Cell Membrane - chemistry
/ Cell Membrane - genetics
/ Cell Membrane - metabolism
/ Coliforms
/ E coli
/ Escherichia coli
/ FtsY
/ Fundamental and applied biological sciences. Psychology
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Immunoblotting
/ Insertion
/ Integral membrane proteins
/ Localization
/ membrane localization
/ Membranes
/ Microbiology
/ Miscellaneous
/ N-Terminus
/ Protein Binding
/ Protein Structure, Tertiary
/ Protein Transport
/ Proteins
/ Receptors, Cytoplasmic and Nuclear - chemistry
/ Receptors, Cytoplasmic and Nuclear - genetics
/ Receptors, Cytoplasmic and Nuclear - metabolism
/ Signal recognition particle
/ Streptomyces coelicolor
/ Streptomyces coelicolor - chemistry
/ Streptomyces coelicolor - genetics
/ Streptomyces coelicolor - metabolism
/ transmembrane structure
2012
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The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization
by
Li, Yongquan
, Shen, Xueling
, Mao, Xuming
, Li, Shanzhen
, Du, Yiling
in
Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Binding
/ Biological and medical sciences
/ Cell Membrane - chemistry
/ Cell Membrane - genetics
/ Cell Membrane - metabolism
/ Coliforms
/ E coli
/ Escherichia coli
/ FtsY
/ Fundamental and applied biological sciences. Psychology
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Immunoblotting
/ Insertion
/ Integral membrane proteins
/ Localization
/ membrane localization
/ Membranes
/ Microbiology
/ Miscellaneous
/ N-Terminus
/ Protein Binding
/ Protein Structure, Tertiary
/ Protein Transport
/ Proteins
/ Receptors, Cytoplasmic and Nuclear - chemistry
/ Receptors, Cytoplasmic and Nuclear - genetics
/ Receptors, Cytoplasmic and Nuclear - metabolism
/ Signal recognition particle
/ Streptomyces coelicolor
/ Streptomyces coelicolor - chemistry
/ Streptomyces coelicolor - genetics
/ Streptomyces coelicolor - metabolism
/ transmembrane structure
2012
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The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization
by
Li, Yongquan
, Shen, Xueling
, Mao, Xuming
, Li, Shanzhen
, Du, Yiling
in
Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Bacteriology
/ Binding
/ Biological and medical sciences
/ Cell Membrane - chemistry
/ Cell Membrane - genetics
/ Cell Membrane - metabolism
/ Coliforms
/ E coli
/ Escherichia coli
/ FtsY
/ Fundamental and applied biological sciences. Psychology
/ Hydrophobic and Hydrophilic Interactions
/ Hydrophobicity
/ Immunoblotting
/ Insertion
/ Integral membrane proteins
/ Localization
/ membrane localization
/ Membranes
/ Microbiology
/ Miscellaneous
/ N-Terminus
/ Protein Binding
/ Protein Structure, Tertiary
/ Protein Transport
/ Proteins
/ Receptors, Cytoplasmic and Nuclear - chemistry
/ Receptors, Cytoplasmic and Nuclear - genetics
/ Receptors, Cytoplasmic and Nuclear - metabolism
/ Signal recognition particle
/ Streptomyces coelicolor
/ Streptomyces coelicolor - chemistry
/ Streptomyces coelicolor - genetics
/ Streptomyces coelicolor - metabolism
/ transmembrane structure
2012
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The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization
Journal Article
The N-terminal hydrophobic segment of Streptomyces coelicolor FtsY forms a transmembrane structure to stabilize its membrane localization
2012
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Overview
Abstract
FtsY is the receptor of the signal recognition particle that mediates the targeting of integral membrane proteins in bacteria. It was shown that in Escherichia coli, the N-terminal region of FtsY contributes to its interaction with the membrane, but it is not inserted into the membrane. However, this study presents evidence that in Streptomyces coelicolor, FtsY has a hydrophobic region at its N-terminus, which forms a membrane insertion structure and contributes significantly to the binding between FtsY and membrane. Through membrane protein extraction followed by immunoblotting, we demonstrated that deletion of the N-terminal residues 11–39 from the S. coelicolor FtsY (ScFtsY) drastically reduced its membrane-binding capability and that the N-terminus of ScFtsY alone was capable of targeting the soluble EGFP protein onto the membrane with high efficiency. Furthermore, in a labeling experiment with the membrane-impermeable probe Mal-PEG, the ScFtsY N-terminal region was protected by the membrane and was not labeled. This observation indicates that this region was inserted into the membrane.
Publisher
Blackwell Publishing Ltd,Wiley-Blackwell,Oxford University Press
Subject
Bacterial Proteins - chemistry
/ Bacterial Proteins - genetics
/ Bacterial Proteins - metabolism
/ Binding
/ Biological and medical sciences
/ E coli
/ FtsY
/ Fundamental and applied biological sciences. Psychology
/ Hydrophobic and Hydrophilic Interactions
/ Proteins
/ Receptors, Cytoplasmic and Nuclear - chemistry
/ Receptors, Cytoplasmic and Nuclear - genetics
/ Receptors, Cytoplasmic and Nuclear - metabolism
/ Streptomyces coelicolor - chemistry
/ Streptomyces coelicolor - genetics
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