Microbiology
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


Microbiology 143 (1997), 2135-2143; DOI  10.1099/00221287-143-7-2135
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Right arrow Citation Map
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via CrossRef
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Lyutzkanova, D.
Right arrow Articles by Altenbuchner, J.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Lyutzkanova, D.
Right arrow Articles by Altenbuchner, J.
Agricola
Right arrow Articles by Lyutzkanova, D.
Right arrow Articles by Altenbuchner, J.

A spectinomyciin resistance determinant from the spectinomycin producerStreptomyces flavopersicus

Dimitrina Lyutzkanova1,{dagger}, Jurgen Distler2 and Josef Altenbuchner1,*

1Institut für Industrielle Genetik, Universität Stuttgart, Allmandring 31, 70569 Stuttgart, Germany
2FB9-Mikrobiologie, Bergische Universität-GH, 42097 Wuppertal, Germany

*Author for correspondence: Josef Altenbuchner. Tel: + 49 711 685 7591. Fax: + 49 711 685 6973. e-mail: joe@genius.biologie.uni-sturcgart.de

ABSTRACT

Summary: The spectinomycin (Sp) resistance determinant from Streptomyces flavopersicus was cloned into Streptomyces lividans using the plasmid vector pIJ699. A plasmid, pDGL15, with a 3.65 kb insert from S. flavopersicus conferring resistance to Sp was isolated. DNA sequence analysis of the 3651 bp DNA insert revealed four open reading frames (ORFs). The amino acid sequence deduced from one ORF (SpcN) showed a high degree of similarity to an aminoglycoside phosphotransferase (StrN) and from a second one (SpcR) to a regulatory protein (StrR) of the streptomycin biosynthesis gene cluster from S. griseus. The two other ORFs were incomplete and the deduced amino acid sequences showed similarities to an amidinotransferase encoded in the streptomycin biosynthesis gene cluster of S. griseus and to the transposase of IS112, respectively. Expression of the spcN gene in E. coli under the control of tac promoter conferred Sp resistance to the cells. An enzymic assay confirmed that the gene product of spcN is an ATP-dependent aminoglycoside phosphotransferase which phosphoryiates Sp and actinamine, the aminocyclitol moiety of Sp.


Keywords: Streptomyces flavopersicus, spectinomycin resistance, spectinomycin phosphotransferase, aminoglycoside antibiotics

{dagger} Present address: Institute of Microbiology, Bulgarian Academy of Sciences, Acad. G. Bonchev str., BL26, Sofia 1113, Bulgaria.




This article has been cited by other articles:


Home page
MicrobiologyHome page
J. M. Neary, A. Powell, L. Gordon, C. Milne, F. Flett, B. Wilkinson, C. P. Smith, and J. Micklefield
An asparagine oxygenase (AsnO) and a 3-hydroxyasparaginyl phosphotransferase (HasP) are involved in the biosynthesis of calcium-dependent lipopeptide antibiotics
Microbiology, March 1, 2007; 153(3): 768 - 776.
[Abstract] [Full Text] [PDF]


Home page
Antimicrob. Agents Chemother.Home page
N. A. Magarvey, B. Haltli, M. He, M. Greenstein, and J. A. Hucul
Biosynthetic Pathway for Mannopeptimycins, Lipoglycopeptide Antibiotics Active against Drug-Resistant Gram-Positive Pathogens.
Antimicrob. Agents Chemother., June 1, 2006; 50(6): 2167 - 2177.
[Abstract] [Full Text] [PDF]


Home page
Clin. Microbiol. Rev.Home page
S. B. Vakulenko and S. Mobashery
Versatility of Aminoglycosides and Prospects for Their Future
Clin. Microbiol. Rev., July 1, 2003; 16(3): 430 - 450.
[Abstract] [Full Text] [PDF]


Home page
Nucleic Acids ResHome page
H. J. Sofia, G. Chen, B. G. Hetzler, J. F. Reyes-Spindola, and N. E. Miller
Radical SAM, a novel protein superfamily linking unresolved steps in familiar biosynthetic pathways with radical mechanisms: functional characterization using new analysis and information visualization methods
Nucleic Acids Res., March 1, 2001; 29(5): 1097 - 1106.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
P. R. Thompson, D. W. Hughes, N. P. Cianciotto, and G. D. Wright
Spectinomycin Kinase from Legionella pneumophila. CHARACTERIZATION OF SUBSTRATE SPECIFICITY AND IDENTIFICATION OF CATALYTICALLY IMPORTANT RESIDUES
J. Biol. Chem., June 12, 1998; 273(24): 14788 - 14795.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
INT J SYST EVOL MICROBIOL MICROBIOLOGY J GEN VIROL
J MED MICROBIOL ALL SGM JOURNALS
Copyright © 1997 Society for General Microbiology.