Biological effect of phosphate on the dissimilatory arsenate-respiring bacteria-catalyzed reductive mobilization of arsenic from contaminated soils.

Dissimilatory arsenate-respiring prokaryotes (DARPs) are considered to be the major drive of the reductive mobilization of arsenic from solid phases. However, it is not fully understood how phosphate, a structural analog of arsenate, affects the DARPs-mediated arsenic mobilization. This work aimed to address this issue. As-contaminated soils were collected from a Shimen Realgar Mine-affected area. We identified a unique diversity of DARPs from the soils, which possess high As(V)-respiring activities using one of multiple small organic acids as the electron donor. After elimination of the desorption effect of phosphate on the As mobilization, the supplement of additional 10 mM phosphate to the active slurries markedly increased the microbial community-mediated reductive mobilization of arsenic as revealed by microcosm tests; this observation was associated to the fact that phosphate significantly increased the As(V)-respiratory reductase (Arr) gene abundances in the slurries. To confirm this finding, we further obtained a new DARP strain, Priestia sp. F01, from the samples. We found that after elimination of the chemical effect of phosphate, the supplement of 10 mM phosphate to the active slurries resulted in an 82.2% increase of the released As(III) in the solutions, which could be contributed to that excessive phosphate greatly increased the Arr gene abundance, and enhanced the transcriptional level of arrA gene and the bacterial As(V)-respiring activity of F01 cells. Considering that phosphate commonly coexists with As in the environment, and is a frequently-used fertilizer, these findings are helpful for deeply understanding why As concentrations in contaminated groundwater are dynamically fluctuated, and also provided new knowledge on the interactions between the biogeochemical processes of P and As.

Molecular and bioinformatical characterization of a novel superfamily of cysteine-rich peptides from arthropods.

The full-length cDNA sequences of two novel cysteine-rich peptides (referred to as HsVx1 and MmKTx1) were obtained from scorpions. The two peptides represent a novel class of cysteine-rich peptides with a unique cysteine pattern. The genomic sequence of HsVx1 is composed of three exons interrupted by two introns that are localized in the mature peptide encoding region and inserted in phase 1 and phase 2, respectively. Such a genomic organization markedly differs from those of other peptides from scorpions described previously. Genome-wide search for the orthologs of HsVx1 identified 59 novel cysteine-rich peptides from arthropods. These peptides share a consistent cysteine pattern with HsVx1. Genomic comparison revealed extensive intron length differences and intronic number and position polymorphisms among the genes of these peptides. Further analysis identified 30 cases of intron sliding, 1 case of intron gain and 22 cases of intron loss occurred with the genes of the HsVx1 and HsVx1-like peptides. It is interesting to see that three HsVx1-like peptides XP_001658928, XP_001658929 and XP_001658930 were derived from a single gene (XP gene): the former two were generated from alternative splicing; the third one was encoded by a DNA region in the reverse complementary strand of the third intron of the XP gene. These findings strongly suggest that the genes of these cysteine-rich peptides were evolved by intron sliding, intron gain/loss, gene recombination and alternative splicing events in response to selective forces without changing their cysteine pattern. The evolution of these genes is dominated by intron sliding and intron loss.