Complete genome sequence of Desulfotomaculum acetoxidans type strain (5575T)
Stefan Spring,Alla Lapidus,Maren Schröder,Dorothea Gleim,David Sims,Linda Meincke,Tijana Glavina del Rio,Hope Tice,Alex Copeland,Jan Fang Cheng,Susan Lucas,Feng Chen,Matt Nolan,David Bruce,David Bruce,Lynne Goodwin,Lynne Goodwin,Sam Pitluck,Natalia Ivanova,Konstantinos Mavromatis,Natalia Mikhailova,Amrita Pati,Amy Chen,Krishna Palaniappan,Miriam Land,Miriam Land,Loren Hauser,Loren Hauser,Yun Juan Chang,Yun Juan Chang,Cynthia D. Jeffries,Cynthia D. Jeffries,Patrick S. G. Chain,Patrick S. G. Chain,Elizabeth Saunders,Elizabeth Saunders,Thomas Brettin,Thomas Brettin,John C. Detter,John C. Detter,Markus Göker,James Bristow,Jonathan A. Eisen,Jonathan A. Eisen,Victor Markowitz,Philip Hugenholtz,Nikos C. Kyrpides,Hans-Peter Klenk,Cliff Han,Cliff Han +49 more
TLDR
This is the first completed genome sequence of a Desulfotomaculum species with validly published name and it is able to oxidize substrates completely to carbon dioxide with sulfate as the electron acceptor, which is reduced to hydrogen sulfide.Abstract:
Desulfotomaculum acetoxidans Widdel and Pfennig 1977 was one of the first sulfate-reducing bacteria known to grow with acetate as sole energy and carbon source. It is able to oxidize substrates completely to carbon dioxide with sulfate as the electron acceptor, which is reduced to hydrogen sulfide. All available data about this species are based on strain 5575T, isolated from piggery waste in Germany. Here we describe the features of this organism, together with the complete genome sequence and annotation. This is the first completed genome sequence of a Desulfotomaculum species with validly published name. The 4,545,624 bp long single replicon genome with its 4370 protein-coding and 100 RNA genes is a part of the Genomic Encyclopedia of Bacteria and Archaea project.read more
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Book ChapterDOI
A Post-Genomic View of the Ecophysiology, Catabolism and Biotechnological Relevance of Sulphate-Reducing Prokaryotes
Ralf Rabus,Sofia S. Venceslau,Lars Wöhlbrand,Gerrit Voordouw,Judy D. Wall,Inês A. C. Pereira +5 more
TL;DR: The wealth of publications in this period is a testimony to the large environmental, biogeochemical and technological relevance of these organisms and how much the field has progressed in these years, although many important questions and applications remain to be explored.
Journal ArticleDOI
Unifying concepts in anaerobic respiration: insights from dissimilatory sulfur metabolism.
TL;DR: Some of the redox proteins involved in dissimilatory sulfur metabolism are reviewed, focusing on sulfate reducing organisms, and links to the complex iron-sulfur molybdoenzyme family, and heterodisulfide reductases of methanogenic archaea are highlighted.
Journal ArticleDOI
How sulphate-reducing microorganisms cope with stress: lessons from systems biology
Jizhong Zhou,Qiang He,Christopher L. Hemme,Aindrila Mukhopadhyay,Kristina L. Hillesland,Aifen Zhou,Zhili He,Joy D. Van Nostrand,Terry C. Hazen,David A. Stahl,Judy D. Wall,Adam P. Arkin +11 more
TL;DR: This Review highlights recent applications of systems biology tools in studying the stress responses of SRMs, particularly Desulfovibrio spp.
Journal ArticleDOI
Short-read assembly of full-length 16S amplicons reveals bacterial diversity in subsurface sediments.
Christopher S. Miller,Kim M. Handley,Kelly C. Wrighton,Kyle R. Frischkorn,Brian C. Thomas,Jillian F. Banfield +5 more
TL;DR: A new version of EMIRGE optimized for large data size is used to reconstruct near-full-length 16S rRNA genes from amplicons sheared and sequenced with Illumina technology, allowing for sensitive, accurate profiling of the “long tail” of low abundance organisms that exist in many microbial communities, and can resolve population dynamics in response to environmental change.
Journal ArticleDOI
The "bacterial heterodisulfide" DsrC is a key protein in dissimilatory sulfur metabolism.
TL;DR: The idea that this protein may serve as a redox hub linking oxidation of several substrates to dissimilative sulfur metabolism is discussed, and a new protein is named RspA (for regulatory sulfur-related protein) that is possibly involved in the regulation of gene expression and does not need the conserved Cys for its function.
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