Characterization of a new peptide transport system in Streptococcus thermophilus
In silico analysis of the genome of Streptococcus thermophilus LMD-9 revealed that this strain has a potential new peptide/nickel ABC transporter. We named this system OTS for Oligopeptide Transporter of S. thermophilus. It is composed of a peptide/nickel binding protein OtsA, two permeases OtsB and...
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| Veröffentlicht in: | Food research international 2016-08, Vol.86, p.34-45 |
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| creator | Jameh, Nawara Galia, Wessam Awussi, Ahoefa Ablavi Roux, Emeline Genay, Magali Perrin, Clarisse Dary-Mourot, Annie |
| description | In silico analysis of the genome of Streptococcus thermophilus LMD-9 revealed that this strain has a potential new peptide/nickel ABC transporter. We named this system OTS for Oligopeptide Transporter of S. thermophilus. It is composed of a peptide/nickel binding protein OtsA, two permeases OtsB and OtsC and a double ATPase OtsD. This system was presumably acquired by horizontal transfer from Actinobacteria or distant species like Lactococcus raffinolactis or Enterococcus asini may be via an intermediate like Lactococcus lactis or its ancestor. RT-PCR experiments proved that OTS gene cluster is transcribed and that at least the otsB, otsC, and otsD genes constitute an operon. A mutant LMD-9Δots, partially deleted for the otsA and otsB genes was constructed. Growth of LMD-9 and LMD-9Δots strains was monitored in the presence of different nitrogen sources and in the presence of urea and nickel. Results revealed that OTS is not implicated in nickel transport, but constitutes a new characterized transporter of peptides of small size, possibly di- and tripeptides in S. thermophilus.
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•Di-tripeptide transport system•Gene acquisition by horizontal transfer event•Proteolytic surface system |
| doi_str_mv | 10.1016/j.foodres.2016.04.039 |
| format | Article |
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•Di-tripeptide transport system•Gene acquisition by horizontal transfer event•Proteolytic surface system</description><identifier>ISSN: 0963-9969</identifier><identifier>EISSN: 1873-7145</identifier><identifier>DOI: 10.1016/j.foodres.2016.04.039</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Actinobacteria ; Enterococcus ; Genes ; Lactococcus ; Lactococcus lactis ; Life Sciences ; Nickel ; Nitrogen ; Nitrogen uptake ; Peptide ABC transporter ; Peptides ; Streptococcus ; Streptococcus thermophilus ; Transport ; Transporter ; Ureas</subject><ispartof>Food research international, 2016-08, Vol.86, p.34-45</ispartof><rights>2016</rights><rights>Distributed under a Creative Commons Attribution 4.0 International License</rights><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c409t-2e1f2cbfbdd485c4d9efcfda9685f0fb0684cd50cf11f32cfb6fceb01586e0803</citedby><cites>FETCH-LOGICAL-c409t-2e1f2cbfbdd485c4d9efcfda9685f0fb0684cd50cf11f32cfb6fceb01586e0803</cites><orcidid>0000-0003-3402-0555 ; 0000-0003-3569-1051 ; 0000-0001-7768-6360 ; 0000-0003-4815-8723</orcidid></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://www.sciencedirect.com/science/article/pii/S0963996916301831$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>230,314,776,780,881,3537,27901,27902,65306</link.rule.ids><backlink>$$Uhttps://hal.science/hal-01533905$$DView record in HAL$$Hfree_for_read</backlink></links><search><creatorcontrib>Jameh, Nawara</creatorcontrib><creatorcontrib>Galia, Wessam</creatorcontrib><creatorcontrib>Awussi, Ahoefa Ablavi</creatorcontrib><creatorcontrib>Roux, Emeline</creatorcontrib><creatorcontrib>Genay, Magali</creatorcontrib><creatorcontrib>Perrin, Clarisse</creatorcontrib><creatorcontrib>Dary-Mourot, Annie</creatorcontrib><title>Characterization of a new peptide transport system in Streptococcus thermophilus</title><title>Food research international</title><description>In silico analysis of the genome of Streptococcus thermophilus LMD-9 revealed that this strain has a potential new peptide/nickel ABC transporter. We named this system OTS for Oligopeptide Transporter of S. thermophilus. It is composed of a peptide/nickel binding protein OtsA, two permeases OtsB and OtsC and a double ATPase OtsD. This system was presumably acquired by horizontal transfer from Actinobacteria or distant species like Lactococcus raffinolactis or Enterococcus asini may be via an intermediate like Lactococcus lactis or its ancestor. RT-PCR experiments proved that OTS gene cluster is transcribed and that at least the otsB, otsC, and otsD genes constitute an operon. A mutant LMD-9Δots, partially deleted for the otsA and otsB genes was constructed. Growth of LMD-9 and LMD-9Δots strains was monitored in the presence of different nitrogen sources and in the presence of urea and nickel. Results revealed that OTS is not implicated in nickel transport, but constitutes a new characterized transporter of peptides of small size, possibly di- and tripeptides in S. thermophilus.
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•Di-tripeptide transport system•Gene acquisition by horizontal transfer event•Proteolytic surface system</description><subject>Actinobacteria</subject><subject>Enterococcus</subject><subject>Genes</subject><subject>Lactococcus</subject><subject>Lactococcus lactis</subject><subject>Life Sciences</subject><subject>Nickel</subject><subject>Nitrogen</subject><subject>Nitrogen uptake</subject><subject>Peptide ABC transporter</subject><subject>Peptides</subject><subject>Streptococcus</subject><subject>Streptococcus thermophilus</subject><subject>Transport</subject><subject>Transporter</subject><subject>Ureas</subject><issn>0963-9969</issn><issn>1873-7145</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2016</creationdate><recordtype>article</recordtype><recordid>eNqNkUFrGzEQhUVpoW7an1DQsT3sZrS7kqVTCCZtAoYU2p6FVhphmfVqI8kp6a-vjEOvyWmYme8Nw3uEfGbQMmDict_6GF3C3Ha1bWFooVdvyIrJdd-s2cDfkhUo0TdKCfWefMh5DwCCr9WK_NjsTDK2YAp_TQlxptFTQ2f8QxdcSnBISzJzXmIqND_lggcaZvqzpLqNNlp7zLTsMB3isgvTMX8k77yZMn56rhfk97ebX5vbZnv__W5zvW3sAKo0HTLf2dGPzg2S28Ep9NY7o4TkHvwIQg7WcbCeMd931o_CWxyBcSkQJPQX5Ov57s5MeknhYNKTjibo2-utPs0q2vcK-COr7Jczu6T4cMRc9CFki9NkZozHrJnseXVDdN0rUMZkJaWsKD-jNsWcE_r_bzDQp2D0Xj8Ho0_BaBh0Dabqrs46rPY8Bkw624CzRRcS2qJdDC9c-Afrh5s1</recordid><startdate>20160801</startdate><enddate>20160801</enddate><creator>Jameh, Nawara</creator><creator>Galia, Wessam</creator><creator>Awussi, Ahoefa Ablavi</creator><creator>Roux, Emeline</creator><creator>Genay, Magali</creator><creator>Perrin, Clarisse</creator><creator>Dary-Mourot, Annie</creator><general>Elsevier Ltd</general><general>Elsevier</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7QL</scope><scope>7ST</scope><scope>C1K</scope><scope>SOI</scope><scope>8FD</scope><scope>F28</scope><scope>FR3</scope><scope>1XC</scope><orcidid>https://orcid.org/0000-0003-3402-0555</orcidid><orcidid>https://orcid.org/0000-0003-3569-1051</orcidid><orcidid>https://orcid.org/0000-0001-7768-6360</orcidid><orcidid>https://orcid.org/0000-0003-4815-8723</orcidid></search><sort><creationdate>20160801</creationdate><title>Characterization of a new peptide transport system in Streptococcus thermophilus</title><author>Jameh, Nawara ; Galia, Wessam ; Awussi, Ahoefa Ablavi ; Roux, Emeline ; Genay, Magali ; Perrin, Clarisse ; Dary-Mourot, Annie</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c409t-2e1f2cbfbdd485c4d9efcfda9685f0fb0684cd50cf11f32cfb6fceb01586e0803</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2016</creationdate><topic>Actinobacteria</topic><topic>Enterococcus</topic><topic>Genes</topic><topic>Lactococcus</topic><topic>Lactococcus lactis</topic><topic>Life Sciences</topic><topic>Nickel</topic><topic>Nitrogen</topic><topic>Nitrogen uptake</topic><topic>Peptide ABC transporter</topic><topic>Peptides</topic><topic>Streptococcus</topic><topic>Streptococcus thermophilus</topic><topic>Transport</topic><topic>Transporter</topic><topic>Ureas</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Jameh, Nawara</creatorcontrib><creatorcontrib>Galia, Wessam</creatorcontrib><creatorcontrib>Awussi, Ahoefa Ablavi</creatorcontrib><creatorcontrib>Roux, Emeline</creatorcontrib><creatorcontrib>Genay, Magali</creatorcontrib><creatorcontrib>Perrin, Clarisse</creatorcontrib><creatorcontrib>Dary-Mourot, Annie</creatorcontrib><collection>CrossRef</collection><collection>Bacteriology Abstracts (Microbiology B)</collection><collection>Environment Abstracts</collection><collection>Environmental Sciences and Pollution Management</collection><collection>Environment Abstracts</collection><collection>Technology Research Database</collection><collection>ANTE: Abstracts in New Technology & Engineering</collection><collection>Engineering Research Database</collection><collection>Hyper Article en Ligne (HAL)</collection><jtitle>Food research international</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Jameh, Nawara</au><au>Galia, Wessam</au><au>Awussi, Ahoefa Ablavi</au><au>Roux, Emeline</au><au>Genay, Magali</au><au>Perrin, Clarisse</au><au>Dary-Mourot, Annie</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Characterization of a new peptide transport system in Streptococcus thermophilus</atitle><jtitle>Food research international</jtitle><date>2016-08-01</date><risdate>2016</risdate><volume>86</volume><spage>34</spage><epage>45</epage><pages>34-45</pages><issn>0963-9969</issn><eissn>1873-7145</eissn><abstract>In silico analysis of the genome of Streptococcus thermophilus LMD-9 revealed that this strain has a potential new peptide/nickel ABC transporter. We named this system OTS for Oligopeptide Transporter of S. thermophilus. It is composed of a peptide/nickel binding protein OtsA, two permeases OtsB and OtsC and a double ATPase OtsD. This system was presumably acquired by horizontal transfer from Actinobacteria or distant species like Lactococcus raffinolactis or Enterococcus asini may be via an intermediate like Lactococcus lactis or its ancestor. RT-PCR experiments proved that OTS gene cluster is transcribed and that at least the otsB, otsC, and otsD genes constitute an operon. A mutant LMD-9Δots, partially deleted for the otsA and otsB genes was constructed. Growth of LMD-9 and LMD-9Δots strains was monitored in the presence of different nitrogen sources and in the presence of urea and nickel. Results revealed that OTS is not implicated in nickel transport, but constitutes a new characterized transporter of peptides of small size, possibly di- and tripeptides in S. thermophilus.
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•Di-tripeptide transport system•Gene acquisition by horizontal transfer event•Proteolytic surface system</abstract><pub>Elsevier Ltd</pub><doi>10.1016/j.foodres.2016.04.039</doi><tpages>12</tpages><orcidid>https://orcid.org/0000-0003-3402-0555</orcidid><orcidid>https://orcid.org/0000-0003-3569-1051</orcidid><orcidid>https://orcid.org/0000-0001-7768-6360</orcidid><orcidid>https://orcid.org/0000-0003-4815-8723</orcidid></addata></record> |
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| subjects | Actinobacteria Enterococcus Genes Lactococcus Lactococcus lactis Life Sciences Nickel Nitrogen Nitrogen uptake Peptide ABC transporter Peptides Streptococcus Streptococcus thermophilus Transport Transporter Ureas |
| title | Characterization of a new peptide transport system in Streptococcus thermophilus |
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