We report on the identification and characterization of two dinucleotide, two trinucleotide and eight tetranucleotide microsatellite DNA loci isolated from the European subterranean termite Reticulitermes santonensis . We tested the loci on 51 -92 individuals from 46 colonies from different regions of France. Eleven loci were polymorphic with 2 -8 alleles per locus and low observed heterozygosities (0.10 -0.48). We also tested the loci on 17 -20 individuals from 10 colonies in the closely related North American species R. flavipes and found significantly more alleles (2 -9 alleles per locus) and higher observed heterozygosities (0.15 -0.80) than in R. santonensis . The lower observed heterozygosities in R. santonensis are consistent with higher levels of inbreeding in these colonies due to the presence of numerous inbred replacement reproductives.

Numerous affinity purification-mass spectrometry (AP-MS) and yeast two-hybrid screens have each defined thousands of pairwise protein-protein interactions (PPIs), most of which are between functionally unrelated proteins. The accuracy of these networks, however, is under debate. Here, we present an AP-MS survey of the bacterium Desulfovibrio vulgaris together with a critical reanalysis of nine published bacterial yeast two-hybrid and AP-MS screens. We have identified 459 high confidence PPIs from D. vulgaris and 391 from Escherichia coli. Compared with the nine published interactomes, our two networks are smaller, are much less highly connected, and have significantly lower false discovery rates. In addition, our interactomes are much more enriched in protein pairs that are encoded in the same operon, have similar functions, and are reproducibly detected in other physical interaction assays than the pairs reported in prior studies. Our work establishes more stringent benchmarks for the properties of protein interactomes and suggests that bona fide PPIs much more frequently involve protein partners that are annotated with similar functions or that can be validated in independent assays than earlier studies suggested. Molecular & Cellular Proteomics

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Due to their adjacent location in the genomes of Desulfovibrio species and their potential for formation of an electron transfer pathway in sulfate-reducing prokaryotes, adenosyl phosphosulfate (APS) reductase (Apr) and quinone-interacting membrane-bound oxidoreductase (Qmo) have been thought to interact together during the reduction of APS. This interaction was recently verified in Desulfovibrio desulfuricans. Membrane proteins of Desulfovibrio vulgaris Hildenborough DqmoABCD JW9021, a deletion mutant, were compared to the parent strain using blue-native PAGE to determine whether Qmo formed a complex with Apr or other proteins. In the parent strain of D. vulgaris, a unique band was observed that contained all four Qmo subunits, and another band contained three subunits of Qmo, as well as subunits of AprA and AprB. Similar results were observed with bands excised from membrane preparations of Desulfovibrio alaskensis strain G20. These results are in support of the formation of a physical complex between the two proteins; a result that was further confirmed by the co-purification of QmoA/B and AprA/B from affinity-tagged D. vulgaris Hildenborough strains (AprA, QmoA and QmoB) regardless of which subunit had been tagged. This provides clear evidence for the presence of a Qmo-Apr complex that is at least partially stable in protein extracts of D. vulgaris and D. alaskensis. INTRODUCTIONSulfate-reducing prokaryotes (SRPs) respire sulphate, and although their entire respiratory process has not been fully elucidated, there has been much progress in determining the role of a number of SRP proteins (Pereira et al., 2007). Current concepts for sulfate respiration involve a range of both intrinsic membrane proteins, as well as soluble cytoplasmic and periplasmic proteins, some of which are required exclusively for H 2 or formate oxidation (Li et al., 2009). The first step in the SRP respiration process involves the reduction of sulfate to sulfite, a two electron reduction. In order for this step to proceed, sulfate must first be converted to adenosyl phosphosulfate (APS) through a reaction involving ATP being carried out by the enzyme, sulfate adenylyltransferase (Sat) (Pereira et al., 2007), which is present in all SRPs (Meyer & Kuever, 2007a). APS reductase (Apr) then catalyses the reduction of APS to sulfite and adenosine monophosphate (Lampreia et al., 1994). The Apr (AprBA) has been purified as a soluble Abbreviations: Apr, adenosyl phosphosulfate reductase; APS, adenosyl phosphosulfate; DDM, dodecyl maltoside; Qmo, quinone-interacting membrane-bound oxidoreductase; Sat, sulfate adenylyltransferase; SRP, sulfate-reducing prokaryote.Supplementary material is available with the online version of this paper. complex with a molecular mass of about 95 kDa and is thought to be arranged in a 1 : 1 a-b heterodimer (Fritz et al., 2000). The a subunit is the catalytic subunit with the FAD-binding region, whereas the b subunit contains a ferredoxin domain that is involved in electron transfer (Fritz et al., 2002).Because of the...

The dissimilatory sulfate-reducing deltaproteobacterium Desulfovibrio vulgaris Hildenborough (ATCC 29579) was chosen by the research collaboration ENIGMA to explore tools and protocols for bringing this anaerobe to model status. Here, we describe a collection of genetic constructs generated by ENIGMA that are available to the research community.