Unknown

Dataset Information

0

Privileged incorporation of selenium as selenocysteine in Lactobacillus reuteri proteins demonstrated by selenium-specific imaging and proteomics.


ABSTRACT: An analytical approach was developed to study the incorporation of selenium (Se), an important trace element involved in the protection of cells from oxidative stress, into the well-known probiotic Lactobacillus reuteri Lb2 BM-DSM 16143. The analyses revealed that about half of the internalized Se was covalently incorporated into soluble proteins. Se-enriched proteins were detected in 2D gels by laser ablation inductively coupled plasma mass spectrometry imaging (LA-ICP MSI) and identified by capillary HPLC with the parallel ICP MS ((78)Se) and electrospray Orbitrap MS/MS detection. On the basis of the identification of 10 richest in selenium proteins, it was demonstrated that selenium was incorporated by the strain exclusively as selenocysteine. Also, the exact location of selenocysteine within the primary sequence was determined. This finding is in a striking contrast to another common nutraceutical, Se-enriched yeast, which incorporates Se principally as selenomethionine.

SUBMITTER: Galano E 

PROVIDER: S-EPMC3734579 | biostudies-literature | 2013 Aug

REPOSITORIES: biostudies-literature

altmetric image

Publications

Privileged incorporation of selenium as selenocysteine in Lactobacillus reuteri proteins demonstrated by selenium-specific imaging and proteomics.

Galano Eugenio E   Mangiapane Erika E   Bianga Juliusz J   Palmese Angelo A   Pessione Enrica E   Szpunar Joanna J   Lobinski Ryszard R   Amoresano Angela A  

Molecular & cellular proteomics : MCP 20130508 8


An analytical approach was developed to study the incorporation of selenium (Se), an important trace element involved in the protection of cells from oxidative stress, into the well-known probiotic Lactobacillus reuteri Lb2 BM-DSM 16143. The analyses revealed that about half of the internalized Se was covalently incorporated into soluble proteins. Se-enriched proteins were detected in 2D gels by laser ablation inductively coupled plasma mass spectrometry imaging (LA-ICP MSI) and identified by ca  ...[more]

Similar Datasets

2013-09-17 | GSE46038 | GEO
2013-09-17 | E-GEOD-46038 | biostudies-arrayexpress
| S-EPMC6289641 | biostudies-literature
| S-EPMC6103685 | biostudies-literature
| S-EPMC2752292 | biostudies-literature
| S-EPMC2746813 | biostudies-literature
| S-EPMC3889603 | biostudies-literature
| S-EPMC193752 | biostudies-literature
| S-EPMC3636253 | biostudies-literature
| S-EPMC4425961 | biostudies-literature