PXD009127

PXD009127 is an original dataset announced via ProteomeXchange.

Title	Transcriptomic and Proteomic Insight into the Mechanism of Cyclooctasulfur- versus Thiosulfate-Oxidation by the Chemolithoautotroph Sulfurimonas denitrificans
Description	Chemoautotrophic bacteria belonging to the genus Sulfurimonas in the class Campylobacteria (formerly classified as Epsilonproteobacteria) play a key role in the sulfur cycle in a variety of oxygen-deficient or –limited and sulfide-rich marine and terrestrial environments. Previously, they were identified as key players in the turnover of zero-valence sulfur, a central intermediate in the marine sulfur cycle, and S. denitrificans was further shown to be able to oxidize cyclooctasulfur. However, at present the mechanism involved in the activation and metabolism of cyclooctasulfur is not known. To this end, we assessed the transcriptome and proteome of S. denitrificans grown with either thiosulfate or cyclooctasulfur as the electron donor. While the overall profiles under the two growth conditions were rather similar, distinct differences were observed that could be attributed to the utilization of cyclooctasulfur. This included a higher abundance of expressed genes and proteins related to attachment in the presence of cyclooctasulfur and the differential expression of the sulfur-oxidation multienzyme complex (SOX). S. denitrificans uses the SOX system for the oxidation of reduced sulfur compounds, including two copies of the sulfur-binding SoxYZ proteins, encoded in two gene clusters: soxABXYZ1 and soxCDYZ2. While the proteins of both operons of the SOX system were detected in the presence of thiosulfate, only proteins of the soxCDYZ2 operon were detected when grown with cylcooctasulfur. Based on these findings a model for the oxidation of cylcooctasulfur is being proposed that might also apply to other Campylobacteria that share the same arrangement of the SOX system. Our results have implications for interpreting metatranscriptomic and -proteomic data and for the observed high level of diversification of soxYZ2 among sulfur-oxidizing Campylobacteria.
HostingRepository	PRIDE
AnnounceDate	2019-07-22
AnnouncementXML	Submission_2019-07-22_08:37:34.xml
DigitalObjectIdentifier	https://dx.doi.org/10.6019/PXD009127
ReviewLevel	Peer-reviewed dataset
DatasetOrigin	Original dataset
RepositorySupport	Supported dataset by repository
PrimarySubmitter	Florian Goetz
SpeciesList	scientific name: Sulfurimonas denitrificans; NCBI TaxID: 39766;
ModificationList	Oxidation
Instrument	LTQ Orbitrap Elite

Revision	Datetime	Status	ChangeLog Entry
0	2018-03-07 01:30:55	ID requested
⏵ 1	2019-07-22 08:37:36	announced

G, ö, tz F, Pjevac P, Markert S, McNichol J, Becher D, Schweder T, Mussmann M, Sievert SM, Transcriptomic and proteomic insight into the mechanism of cyclooctasulfur- versus thiosulfate-oxidation by the chemolithoautotroph Sulfurimonas denitrificans. Environ Microbiol, 21(1):244-258(2019) [pubmed]

curator keyword: Biological

submitter keyword: Proteomics, Campylobacteria, Epsilonproteobacteria, Sulfur, Oxidation

Stefan M. Sievert
contact affiliation	Department of Biology,Watson Building 207, MS #52, Woods Hole Oceanographic Institution, Woods Hole, MA 02543, USA
contact email	ssievert@whoi.edu
lab head
Florian Goetz
contact affiliation	Phd-candidate
contact email	florian.goetz@hotmail.de
dataset submitter

Dataset FTP location NOTE: Most web browsers have now discontinued native support for FTP access within the browser window. But you can usually install another FTP app (we recommend FileZilla) and configure your browser to launch the external application when you click on this FTP link. Or otherwise, launch an app that supports FTP (like FileZilla) and use this address: ftp://ftp.pride.ebi.ac.uk/pride/data/archive/2019/07/PXD009127

PRIDE project URI

• PRIDE
  1. PXD009127
     1. Label: PRIDE project
     2. Name: Transcriptomic and Proteomic Insight into the Mechanism of Cyclooctasulfur- versus Thiosulfate-Oxidation by the Chemolithoautotroph Sulfurimonas denitrificans