Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU
<p>Abstract</p> <p>Background</p> <p><it>Enterobacter </it>sp. YSU is resistant to several different heavy metal salts, including selenite. A previous study using M-9 minimal medium showed that when the selenite concentration was 100,000 times higher than th...
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doaj-d308bacea2324693a0c9ead150d2f58b2020-11-24T21:33:53ZengBMCProteome Science1477-59562009-08-01713010.1186/1477-5956-7-30Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSUKonda VenkataramanaMoparthi SwarnalathaShaik NabeelKulkarni SamathaBarasa NathanielJasenec AshleyCaguiat Jonathan<p>Abstract</p> <p>Background</p> <p><it>Enterobacter </it>sp. YSU is resistant to several different heavy metal salts, including selenite. A previous study using M-9 minimal medium showed that when the selenite concentration was 100,000 times higher than the sulfate concentration, selenite entered <it>Escherichia coli </it>cells using two pathways: a specific and a non-specific pathway. In the specific pathway, selenite entered the cells through a yet to be characterized channel dedicated for selenite. In the non-specific pathway, selenite entered the cells through a sulfate permease channel. Addition of L-cystine, an L-cysteine dimer, appeared to indirectly decrease selenite import into the cell through the non-specific pathway. However, it did not affect the level of selenite transport into the cell through the specific pathway.</p> <p>Results</p> <p>Growth curves using M-9 minimal medium containing 40 mM selenite and 1 mM sulfate showed that <it>Enterobacter </it>sp. YSU grew when L-cysteine was present but died when it was absent. Differential protein expression analysis by two dimensional gel electrophoresis showed that CysK was present in cultures containing selenite and lacking L-cysteine but absent in cultures containing both selenite and L-cysteine. Additional RT-PCR studies demonstrated that transcripts for the sulfate permease genes, <it>cysA</it>, <it>cysT </it>and <it>cysW</it>, were down-regulated in the presence of L-cysteine.</p> <p>Conclusion</p> <p>L-cysteine appeared to confer selenite resistance upon <it>Enterobacter sp. </it>YSU by decreasing the level of selenite transport into the cell through the non-specific pathway.</p> http://www.proteomesci.com/content/7/1/30 |
collection |
DOAJ |
language |
English |
format |
Article |
sources |
DOAJ |
author |
Konda Venkataramana Moparthi Swarnalatha Shaik Nabeel Kulkarni Samatha Barasa Nathaniel Jasenec Ashley Caguiat Jonathan |
spellingShingle |
Konda Venkataramana Moparthi Swarnalatha Shaik Nabeel Kulkarni Samatha Barasa Nathaniel Jasenec Ashley Caguiat Jonathan Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU Proteome Science |
author_facet |
Konda Venkataramana Moparthi Swarnalatha Shaik Nabeel Kulkarni Samatha Barasa Nathaniel Jasenec Ashley Caguiat Jonathan |
author_sort |
Konda Venkataramana |
title |
Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU |
title_short |
Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU |
title_full |
Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU |
title_fullStr |
Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU |
title_full_unstemmed |
Proteomic profiling of L-cysteine induced selenite resistance in <it>Enterobacter </it>sp. YSU |
title_sort |
proteomic profiling of l-cysteine induced selenite resistance in <it>enterobacter </it>sp. ysu |
publisher |
BMC |
series |
Proteome Science |
issn |
1477-5956 |
publishDate |
2009-08-01 |
description |
<p>Abstract</p> <p>Background</p> <p><it>Enterobacter </it>sp. YSU is resistant to several different heavy metal salts, including selenite. A previous study using M-9 minimal medium showed that when the selenite concentration was 100,000 times higher than the sulfate concentration, selenite entered <it>Escherichia coli </it>cells using two pathways: a specific and a non-specific pathway. In the specific pathway, selenite entered the cells through a yet to be characterized channel dedicated for selenite. In the non-specific pathway, selenite entered the cells through a sulfate permease channel. Addition of L-cystine, an L-cysteine dimer, appeared to indirectly decrease selenite import into the cell through the non-specific pathway. However, it did not affect the level of selenite transport into the cell through the specific pathway.</p> <p>Results</p> <p>Growth curves using M-9 minimal medium containing 40 mM selenite and 1 mM sulfate showed that <it>Enterobacter </it>sp. YSU grew when L-cysteine was present but died when it was absent. Differential protein expression analysis by two dimensional gel electrophoresis showed that CysK was present in cultures containing selenite and lacking L-cysteine but absent in cultures containing both selenite and L-cysteine. Additional RT-PCR studies demonstrated that transcripts for the sulfate permease genes, <it>cysA</it>, <it>cysT </it>and <it>cysW</it>, were down-regulated in the presence of L-cysteine.</p> <p>Conclusion</p> <p>L-cysteine appeared to confer selenite resistance upon <it>Enterobacter sp. </it>YSU by decreasing the level of selenite transport into the cell through the non-specific pathway.</p> |
url |
http://www.proteomesci.com/content/7/1/30 |
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