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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Main Authors: Konda Venkataramana, Moparthi Swarnalatha, Shaik Nabeel, Kulkarni Samatha, Barasa Nathaniel, Jasenec Ashley, Caguiat Jonathan
Format: Article
Language:English
Published: BMC 2009-08-01
Series:Proteome Science
Online Access:http://www.proteomesci.com/content/7/1/30
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spelling 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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