Molecules and Cells

Korean Society for Molecular and Cellular Biology (한국분자세포생물학회)
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Conformational Change of Escherichia coli Signal Recognition Particle Ffh Is Affected by the Functionality of Signal Peptides of Ribose-Binding Protein

  • Ahn, Taeho (Department of Biochemistry, College of Veterinary Medicine, Chonnam National University) ;
  • Ko, Ju Hee (Department of Biochemistry, College of Veterinary Medicine, Chonnam National University) ;
  • Cho, Eun Yi (School of Biological Sciences and Technology, Chonnam National University) ;
  • Yun, Chul-Ho (School of Biological Sciences and Technology, Chonnam National University)
  • Received : 2009.03.18
  • Accepted : 2009.05.18
  • Published : 2009.06.30
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Abstract

We examined the effects of synthetic signal peptides, wild-type (WT) and export-defective mutant (MT) of ribose-binding protein, on the conformational changes of signal recognition particle 54 homologue (Ffh) in Escherichia coli. Upon interaction of Ffh with WT peptide, the intrinsic Tyr fluorescence, the transition temperature of thermal unfolding, and the GTPase activity of Ffh decreased in a peptide concentration-dependent manner, while the emission intensity of 8-anilinonaphthalene-1-sulfonic acid increased. In contrast, the secondary structure of the protein was not affected. Additionally, polarization of fluorescein-labeled WT increased upon association with Ffh. These results suggest that WT peptide induces the unfolded states of Ffh. The WT-mediated conformational change of Ffh was also revealed to be important in the interaction between SecA and Ffh. However, MT had marginal effect on these conformational changes suggesting that the in vivo functionality of signal peptide is important in the interaction with Ffh and concomitant structural change of the protein.

Keywords

Acknowledgement

Supported by : Korea Research Foundation

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