Journal of Microbiology and Biotechnology

The Korean Society for Microbiology and Biotechnology (한국미생물·생명공학회)
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Important Features for Protein Foldings in Two Acyl Carrier Proteins from Enterococcus faecalis

  • Seoyeong Yoo (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Jiwon Yeon (Department of Bioscience and Biotechnology, Konkuk University) ;
  • Eunhee Kim (Center for Research Equipment, Korea Basic Science Institute) ;
  • Yangmee Kim (Department of Bioscience and Biotechnology, Konkuk University)
  • Received : 2023.09.05
  • Accepted : 2023.09.14
  • Published : 2024.01.28
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Abstract

The emergence of multi-drug resistant Enterococcus faecalis raises a serious threat to global public health. E. faecalis is a gram-positive intestinal commensal bacterium found in humans. E. faecalis can endure extreme environments such as high temperature, pressure, and high salt, which facilitates them to cause infection in hospitals. E. faecalis has two acyl carrier proteins, AcpA (EfAcpA) in de novo fatty acid synthesis (FAS) and AcpB (EfAcpB) which utilizes exogenous fatty acids. Previously, we determined the tertiary structures of these two ACPs and investigated their structure-function relationships. Solution structures revealed that overall folding of these two ACPs is similar to those of other bacterial ACPs. However, circular dichroism (CD) experiments showed that the melting temperature of EfAcpA is 76.3℃ and that of EfAcpB is 79.2℃, which are much higher than those of other bacterial ACPs. In this study, to understand the origin of their structural stabilities, we verified the important residues for stable folding of these two ACPs by monitoring thermal and chemical denaturation. Hydrogen/deuterium exchange and chemical denaturation experiments on wild-type and mutant proteins revealed that Ile10 of EfAcpA and Ile14 of EfAcpB mediate compact intramolecular packing and promote high thermostability and stable folding. E. faecalis may maximize efficiency of FAS and increase adaptability to the environmental stress by having two thermostable ACPs. This study may provide insight into bacterial adaptability and development of antibiotics against multi-drug-resistant E. faecalis.

Keywords

Acknowledgement

This work was supported by a National Research Foundation of Korea (NRF) grant funded by the Korean government (MSIT) (No. RS-2023-00207959) and by the Korea Basic Science Institute under the R&D program (Project No. C330430) supervised by the Ministry of Science and ICT.

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