Shrimp survival in BYOES under the period of 20 months.

<p>(A) The median number of shrimp in BYOES over the observation period of 20 months as well as the Student’s t-test (two-tailed, unpaired) results for each deuterium content. 150 ppm corresponds to normal terrestrial deuterium content. (B) The survival plots after 3-point smoothing. The number of shrimp that were still alive after 20 months was subtracted for each D content and the obtained value renormalized to day 1.</p

Maximum growth rate, lag time and maximum density of aged <i>E. coli</i>.

<p>(<b>A</b>) Maximum growth rate of aged <i>E. coli</i> grown in M9 minimal media with ultralow composition of deuterium. * denotes p<0.05. (<b>B</b>) Lag time of aged <i>E. coli</i> grown in M9 minimal media with ultralow composition of deuterium. (<b>C</b>) Maximum density of aged <i>E. coli</i> grown in M9 minimal media with ultralow composition of deuterium. * denotes p<0.05.</p

Maximum growth rate, lag time, maximum density of <i>E. coli</i> grown in minimal media.

<p>(<b>A</b>) Blue circles: maximum growth rate of <i>E. coli</i> grown in M9 minimal media normalized by that at normal deuterium content of 156 ppm. * denotes p<0.05, ** - p<0.005, etc. Brown squares: predicted maximum growth rate calculated according to the maximum growth rate of <i>E. coli</i> grown in 50% of deuterium. (<b>B</b>) Blue circles: lag time of <i>E. coli</i> grown in M9 minimal media normalized by that at terrestrial content of deuterium from 156 ppm (terrestrial value) to 8%. Inset shows a zoom-in of the ultralow enrichment region. Brown squares: predicted lag time calculated according to the lag time of <i>E. coli</i> grown in 50% of deuterium. (<b>C</b>) Blue circles: maximum density of <i>E. coli</i> grown in M9 minimal media normalized by that at terrestrial deuterium content from 156 ppm (terrestrial value) to 8%. Inset shows a zoom-in of the ultralow enrichment region. Brown squares: predicted maximum density calculated according to maximum density of <i>E. coli</i> grown in 50% of deuterium.</p

Typical growth curve and the three growth parameters derived from the curve.

<p>Typical growth curve and the three growth parameters derived from the curve.</p

The results of <i>E</i>. <i>coli</i> growth parameter measurements at 25°C summarizing two independent experiments, each on a separate 100-well plate.

<p>(A) Maximum growth rate. (B) Maximum density. (C) Lag time. Usually, more advantageous growth conditions result in faster growth, higher maximum density and shorter lag time.</p

Isotopic compositions of the minimal media for conditions of Mars, Venus, Control-All (identical to Earth) and Control-D.

<p>Isotopic compositions of the minimal media for conditions of Mars, Venus, Control-All (identical to Earth) and Control-D.</p

Experimental workflow.

<p>For each plate, 32 samples (S_A) and 32 standards were prepared. Stock A was used for preparing 32 samples on plate P_A. * Milli-Q water was used instead of heavy water to prepare stock solution for the preparation of standards.</p

Stock solutions and their corresponding D content in the final samples.

<p>Stock solution (column one) was prepared by mixing M9 minimal media and heavy water at a certain ratio that resulted in the final D content in the sample (column four). For each sample, stock solution for its corresponding standards (below it is called stock solution of standard X) was prepared in the same way but using Milli-Q water instead of heavy water.</p

Expression levels of the XMRV viral proteins within the proteome of the human cell line LNCaP.

<p>Small red dots correspond to the host cell proteins, whereas the two identified viral proteins are marked as cyan circles. Detected sequences of tryptic peptides of the two viral proteins are marked with color: red - peptides mapped perfectly on the XMRV sequence; blue and green - mutated sequences.</p

Brain Proteomics Supports the Role of Glutamate Metabolism and Suggests Other Metabolic Alterations in Protein l‑Isoaspartyl Methyltransferase (PIMT)-Knockout Mice

Protein l-isoaspartyl methyltransferase (PIMT) repairs the isoaspartyl residues (isoAsp) that originate from asparagine deamidation and aspartic acid (Asp) isomerization to Asp residues. Deletion of the gene encoding PIMT in mice (<i>Pcmt1</i>) leads to isoAsp accumulation in all tissues measured, especially in the brain. These PIMT-knockout (PIMT-KO) mice have perturbed glutamate metabolism and die prematurely of epileptic seizures. To elucidate the role of PIMT further, brain proteomes of PIMT-KO mice and controls were analyzed. The isoAsp levels from two of the detected 67 isoAsp sites (residue 98 from calmodulin and 68 from glyceraldehyde-3-phosphate dehydrogenase) were quantified and found to be significantly increased in PIMT-KO mice (<i>p</i> < 0.01). Additionally, the abundance of at least 151 out of the 1017 quantified proteins was found to be altered in PIMT-KO mouse brains. Gene ontology analysis revealed that many down-regulated proteins are involved in cellular amino acid biosynthesis. For example, the serine synthesis pathway was suppressed, possibly leading to reduced serine production in PIMT-KO mice. Additionally, the abundances of enzymes in the glutamate–glutamine cycle were altered toward the accumulation of glutamate. These findings support the involvement of PIMT in glutamate metabolism and suggest that the absence of PIMT also affects other processes involving amino acid synthesis and metabolism