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In Vivo Characterization of Phosphotransferase-Encoding Genes istP and forP as Interchangeable Launchers of the C3 ',4 '-Dideoxygenation Biosynthetic Pathway of 1,4-Diaminocyclitol Antibiotics

Authors
Nguyen Lan HuongLee, Na JoonHwang, Hyun HaSon, Hye BinKim, Hye JiSeo, Eun GyoNguyen Huu HoangPark, Je Won
Issue Date
3월-2019
Publisher
KOREAN SOC MICROBIOLOGY & BIOTECHNOLOGY
Keywords
Aminoglycoside; istamycin; fortimicin; istP; 3 ' , 4 ' -didehydroxylation; 1-O-methyl-FOR-KK1
Citation
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY, v.29, no.3, pp.367 - 372
Indexed
SCIE
SCOPUS
KCI
Journal Title
JOURNAL OF MICROBIOLOGY AND BIOTECHNOLOGY
Volume
29
Number
3
Start Page
367
End Page
372
URI
https://scholar.korea.ac.kr/handle/2021.sw.korea/67062
DOI
10.4014/jmb.1809.09021
ISSN
1017-7825
Abstract
Deactivation of aminoglycosides by their modifying enzymes, including a number of aminoglycoside O-phosphotransferases, is the most ubiquitous resistance mechanism in aminoglycoside-resistant pathogens. Nonetheless, in a couple of biosynthetic pathways for gentamicins, fortimicins, and istamycins, phosphorylation of aminoglycosides seems to be a unique and initial step for the creation of a natural defensive structural feature such as a 3 ', 4 '-dideoxy scaffold. Our aim was to elucidate the biochemical details on the beginning of these C3 ', 4 '-dideoxygenation biosynthetic steps for aminoglycosides. The biosynthesis of istamycins must surely involve these 3 ', 4 '-didehydroxylation steps, but much less has been reported in terms of characterization of istamycin biosynthetic genes, especially about the phosphotransferase-encoding gene. In the disruption and complementation experiments pointing to a putative gene, istP, in the genome of wild-type Streptomyces tenjimariensis, the function of the istP gene was proved here to be a phosphotransferase. Next, an in-frame deletion of a known phosphotransferase-encoding gene forP from the genome of wild-type Micromonospora olivasterospora resulted in the appearance of a hitherto unidentified fortimicin shunt product, namely 3-O-methyl-FOR-KK1, whereas complementation of forP restored the natural fortimicin metabolite profiles. The bilateral complementation of an istP gene (or forP) in the Delta forP mutant (or Delta istP mutant strain) successfully restored the biosynthesis of 3 ', 4 '-dideoxy fortimicins and istamycins, thus clearly indicating that they are interchangeable launchers of the biosynthesis of 3 ', 4 '-dideoxy types of 1,4-diaminocyclitol antibiotics.
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