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The diversity of FtsY-lipid interactions.

Publication ,  Journal Article
Reinau, ME; Thøgersen, IB; Enghild, JJ; Nielsen, KL; Otzen, DE
Published in: Biopolymers
July 2010

The bacterial signal recognition particle (SRP) receptor FtsY forms a complex with the SRP Ffh to target nascent polypeptide chains to the bacterial inner membrane. How FtsY interacts with lipids and associates to the membrane is unclear. Here, we show that vesicle binding leads to partial protection against proteolytic degradation and a change in secondary structure, which differs depending on whether the lipids are simple mixtures of zwitterionic and anionic lipids, mimics of Escherichia coli lipids, or lysolipids. Lipid binding alters the stability of FtsY. Thermal unfolding of FtsY in buffer shows two transitions, one occurring at approximately 60 degrees C and the other at approximately 90 degrees C. The thermal intermediate accumulating between 60 and 90 degrees C has structural features in common with the state induced by binding to E. coli lipids. E. coli lipid extract induces a single transition around 70 degrees C, anionic lipids have no effect while cooperative unfolding is completely removed in lysolipids. Thus, the lipid environment profoundly influences the dynamic properties of FtsY, leading to three different kinds of FtsY-lipid interactions with different effects on structure, proteolytic protection, and stability, and is driven both by hydrophobic and electrostatic interactions. Trypsin digestion experiments highlight the central role of the N-domain in lipid contacts, whereas the A- and G-domains appear to play a more minor part.

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Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

July 2010

Volume

93

Issue

7

Start / End Page

595 / 606

Related Subject Headings

  • Trypsin
  • Signal Recognition Particle
  • Receptors, Cytoplasmic and Nuclear
  • Protein Structure, Tertiary
  • Protein Folding
  • Membrane Lipids
  • Escherichia coli
  • Biophysics
  • Bacterial Proteins
  • 34 Chemical sciences
 

Citation

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Reinau, M. E., Thøgersen, I. B., Enghild, J. J., Nielsen, K. L., & Otzen, D. E. (2010). The diversity of FtsY-lipid interactions. Biopolymers, 93(7), 595–606. https://doi.org/10.1002/bip.21404
Reinau, M. E., I. B. Thøgersen, J. J. Enghild, K. L. Nielsen, and D. E. Otzen. “The diversity of FtsY-lipid interactions.Biopolymers 93, no. 7 (July 2010): 595–606. https://doi.org/10.1002/bip.21404.
Reinau ME, Thøgersen IB, Enghild JJ, Nielsen KL, Otzen DE. The diversity of FtsY-lipid interactions. Biopolymers. 2010 Jul;93(7):595–606.
Reinau, M. E., et al. “The diversity of FtsY-lipid interactions.Biopolymers, vol. 93, no. 7, July 2010, pp. 595–606. Epmc, doi:10.1002/bip.21404.
Reinau ME, Thøgersen IB, Enghild JJ, Nielsen KL, Otzen DE. The diversity of FtsY-lipid interactions. Biopolymers. 2010 Jul;93(7):595–606.
Journal cover image

Published In

Biopolymers

DOI

EISSN

1097-0282

ISSN

0006-3525

Publication Date

July 2010

Volume

93

Issue

7

Start / End Page

595 / 606

Related Subject Headings

  • Trypsin
  • Signal Recognition Particle
  • Receptors, Cytoplasmic and Nuclear
  • Protein Structure, Tertiary
  • Protein Folding
  • Membrane Lipids
  • Escherichia coli
  • Biophysics
  • Bacterial Proteins
  • 34 Chemical sciences