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논문 기본 정보

자료유형
학술저널
저자정보
Yoo Seoyeong (Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea) Yeon Jiwon (Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea) Kim Eunhee (Center for Research Equipment, Korea Basic Science Institute, Cheongwon-gun, Chungbuk 363-883, Republic of Korea) Kim Yangmee (Department of Bioscience and Biotechnology, Konkuk University, Seoul 05029, Republic of Korea)
저널정보
한국미생물생명공학회 Journal of Microbiology and Biotechnology Journal of Microbiology and Biotechnology Vol.34 No.1
발행연도
2024.1
수록면
10 - 16 (7page)
DOI
10.4014/jmb.2309.09006

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초록· 키워드

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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°C and that of EfAcpB is 79.2°C, 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.

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