Phosphorylation of chloramphenicol by a recombinant protein Yhr2 from Streptomyces avermitilis MA4680 |
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| Authors: | Thangamani Rajesh Changmin Sung Hyeonjeong Kim Eunjung Song Hyung-Yeon Park Jong-Min Jeon Dongwon Yoo Hyun Joong Kim Yong Hyun Kim Kwon-Young Choi Kyung-Guen Song Yung-Hun Yang |
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| Affiliation: | 1. Department of Microbial Engineering, College of Engineering, Konkuk University, 1 Hwayang-dong, Gwangjin-gu, Seoul 143-701, South Korea;2. Interdisciplinary Program for Bioengineering, Seoul National University, Kwanak-Gu, Seoul 151-742, South Korea;3. Bioengineering Institute, and Institute of Molecular Biology and Genetics, Seoul National University, Gwanak-gu, Seoul 151-742, South Korea;4. School of Chemical and Biological Engineering, Seoul National University, Kwanak-Gu, Seoul 151-742, South Korea;5. Bio-MAX Institute, Seoul National University, Gwanak-gu, Seoul 151-742, South Korea;6. Center for Water Resource Cycle Research, Korea Institute of Science and Technology, 39-1 Hawalgok-dong, Seongbuk-gu, Seoul, South Korea;7. Institute for Ubiquitous Information Technology and Applications (CBRU), Konkuk University, Seoul 143-701, South Korea |
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| Abstract: | ![]()
Although phosphorylation of chloramphenicol has been shown to occur in the chloramphenicol producer, Streptomyces venezuelae, there are no reports on the existence of chloramphenicol phosphorylase in other Streptomyces species. In the present study, we report the modification of chloramphenicol by a recombinant protein, designated as Yhr2 (encoded by SAV_877), from Streptomyces avermitilis MA4680. Recombinant Yhr2 was expressed in Escherichia coli BL21 (DE3) and the cells expressing this recombinant protein were shown to phosphorylate chloramphenicol to a 3′-O-phosphoryl ester derivative, resulting in an inactivated form of the antibiotic. Expression of yhr2 conferred chloramphenicol resistance to E. coli cells up to 25 μg/mL and in an in vitro reaction, adenosine triphosphate (ATP), guanosine triphosphate (GTP), adenosine diphosphate (ADP) and guanosine diphosphate (GDP) were shown to be the phosphate donors for phosphorylation of chloramphenicol. This study highlights that antibiotic resistance conferring genes could be easily expressed and functionalized in other organisms that do not produce the respective antibiotic. |
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| Keywords: | Chloramphenicol phosphorylase Antibiotic modification Heterologous expression Antibiotic resistance |
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