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Mol. Cells 2009; 27(1): 83-88

Published online January 31, 2009

https://doi.org/10.1007/s10059-009-0008-0

© The Korean Society for Molecular and Cellular Biology

Characterization of RbmD (Glycosyltransferase in Ribostamycin Gene Cluster) through Neomycin Production Reconstituted from the Engineered Streptomyces fradiae BS1

Keshav Kumar Nepal, Tae-Jin Oh, Bimala Subba, Jin Cheol Yoo and Jae Kyung Sohng

Received: September 10, 2008; Revised: October 15, 2008; Accepted: October 16, 2008

Abstract

Amino acid homology analysis predicted that rbmD, a putative glycosyltransferase from Streptomyces ribosidificus ATCC 21294, has the highest homology with neoD in neomycin biosynthesis. S. fradiae BS1, in which the production of neomycin was abolished, was generated by disruption of the neoD gene in the neomycin producer S. fradiae. The restoration of neomycin by self complementation suggested that there was no polar effect in the mutant. In addition, S. fradiae BS6 was created with complementation by rbmD in S. fradiae BS1, and secondary metabolite analysis by ESI/MS, LC/MS and MS/MS showed the restoration of neomycin production in S. fradiae BS6. These gene inactivation and complementation studies suggested that, like neoD, rbmD functions as a 2-N-acetlyglucosaminyltransferase and demonstrated the potential for the generation of novel aminoglycoside antibiotics using glycosyltransferases in vivo.

Keywords aminoglycoside, glycosyltransferase, neomycin, ribostamycin, Streptomyces

Article

Research Article

Mol. Cells 2009; 27(1): 83-88

Published online January 31, 2009 https://doi.org/10.1007/s10059-009-0008-0

Copyright © The Korean Society for Molecular and Cellular Biology.

Characterization of RbmD (Glycosyltransferase in Ribostamycin Gene Cluster) through Neomycin Production Reconstituted from the Engineered Streptomyces fradiae BS1

Keshav Kumar Nepal, Tae-Jin Oh, Bimala Subba, Jin Cheol Yoo and Jae Kyung Sohng

Received: September 10, 2008; Revised: October 15, 2008; Accepted: October 16, 2008

Abstract

Amino acid homology analysis predicted that rbmD, a putative glycosyltransferase from Streptomyces ribosidificus ATCC 21294, has the highest homology with neoD in neomycin biosynthesis. S. fradiae BS1, in which the production of neomycin was abolished, was generated by disruption of the neoD gene in the neomycin producer S. fradiae. The restoration of neomycin by self complementation suggested that there was no polar effect in the mutant. In addition, S. fradiae BS6 was created with complementation by rbmD in S. fradiae BS1, and secondary metabolite analysis by ESI/MS, LC/MS and MS/MS showed the restoration of neomycin production in S. fradiae BS6. These gene inactivation and complementation studies suggested that, like neoD, rbmD functions as a 2-N-acetlyglucosaminyltransferase and demonstrated the potential for the generation of novel aminoglycoside antibiotics using glycosyltransferases in vivo.

Keywords: aminoglycoside, glycosyltransferase, neomycin, ribostamycin, Streptomyces

Mol. Cells
Aug 31, 2022 Vol.45 No.8, pp. 513~602
COVER PICTURE
Cryo-EM structure of human porphyrin transporter ABCB6 (main figure) shows that binding of hemin (inset, magenta) in concert with two glutathione molecules (cyan) primes ABCB6 for high ATP turnover (Kim et al., pp. 575-587).

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