A novel taxonomic marker that discriminates between morphologically complex actinomycetes

Girard, Geneviève, Traag, Bjørn A, Sangal, Vartul, Mascini, Nadine, Hoskisson, Paul, Goodfellow, Michael and van Wezel, Gilles (2013) A novel taxonomic marker that discriminates between morphologically complex actinomycetes. Open Biology, 3 (10). p. 130073. ISSN 2046-2441

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Official URL: http://dx.doi.org/10.1098/rsob.130073

Abstract

In the era when large whole genome bacterial datasets are generated routinely, rapid and accurate molecular systematics is becoming increasingly important. However, 16S ribosomal RNA sequencing does not always offer sufficient resolution to discriminate between closely related genera. The SsgA-like proteins are developmental regulatory proteins in sporulating actinomycetes, whereby SsgB actively recruits FtsZ during sporulation-specific cell division. Here, we present a novel method to classify actinomycetes, based on the extraordinary way the SsgA and SsgB proteins are conserved. The almost complete conservation of the SsgB amino acid (aa) sequence between members of the same genus and its high divergence between even closely related genera provides high-quality data for the classification of morphologically complex actinomycetes. Our analysis validates Kitasatospora as a sister genus to Streptomyces in the family Streptomycetaceae and suggests that Micromonospora, Salinispora and Verrucosispora may represent different clades of the same genus. It is also apparent that the aa sequence of SsgA is an accurate determinant for the ability of streptomycetes to produce submerged spores, dividing the phylogenetic tree of streptomycetes into liquid-culture sporulation and no liquid-culture sporulation branches. A new phylogenetic tree of industrially relevant actinomycetes is presented and compared with that based on 16S rRNA sequences.

Item Type: Article
Uncontrolled Keywords: streptomyces,cell division,systematics,genome sequencing
Subjects: C500 Microbiology
C700 Molecular Biology, Biophysics and Biochemistry
Department: Faculties > Health and Life Sciences > Applied Sciences
Depositing User: Vartul Sangal
Date Deposited: 08 Nov 2013 16:36
Last Modified: 24 Oct 2017 11:25
URI: http://nrl.northumbria.ac.uk/id/eprint/14524

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