Structural introspection of a putative fluoride transporter in plants
The xenobiotic fluoride is a detrimental toxin which is exported by a double-barrelled fluoride channel (Fluc) in prokaryotes and a single-barrelled fluoride exporter (FEX) in lower eukaryotes. The presence of FEX gene in higher plant species has not been reported till date. In this communication, w...
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description | The xenobiotic fluoride is a detrimental toxin which is exported by a double-barrelled fluoride channel (Fluc) in prokaryotes and a single-barrelled fluoride exporter (FEX) in lower eukaryotes. The presence of
FEX
gene in higher plant species has not been reported till date. In this communication, we have identified FEXs across nine plant species belonging to five different families. Homology modelling predicted the sequential and structural conservation of crucial residues in plant FEXs. It was predicted that the N-terminal segments were the main target sites for phosphorylation. Other post-translational modifications included Arg methylation, Lys acetylation and Cys
S
-nitrosylation, all of which contribute to protein stability and function. FEXs were predicted to contain lipid moieties which anchor the transporters to the plasma membrane. The crystallizability along with associated properties of plant FEXs was also analyzed to facilitate future experimental analyses. The predicted RNA structure of
OsFEX
formed several pseudoknots, though no riboswitches could be detected from our prediction. The analysis of upstream regions of
FEX
in representative plants represented that this gene could be responsive to phytohormone-mediated signaling. This is the first novel report highlighting that
FEX
genes in plants are probably expressed in a tissue-specific pattern and possibly via a phytohormone-dependent pathway to encode functional FEX proteins during fluoride stress. |
doi_str_mv | 10.1007/s13205-019-1629-4 |
format | Article |
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FEX
gene in higher plant species has not been reported till date. In this communication, we have identified FEXs across nine plant species belonging to five different families. Homology modelling predicted the sequential and structural conservation of crucial residues in plant FEXs. It was predicted that the N-terminal segments were the main target sites for phosphorylation. Other post-translational modifications included Arg methylation, Lys acetylation and Cys
S
-nitrosylation, all of which contribute to protein stability and function. FEXs were predicted to contain lipid moieties which anchor the transporters to the plasma membrane. The crystallizability along with associated properties of plant FEXs was also analyzed to facilitate future experimental analyses. The predicted RNA structure of
OsFEX
formed several pseudoknots, though no riboswitches could be detected from our prediction. The analysis of upstream regions of
FEX
in representative plants represented that this gene could be responsive to phytohormone-mediated signaling. This is the first novel report highlighting that
FEX
genes in plants are probably expressed in a tissue-specific pattern and possibly via a phytohormone-dependent pathway to encode functional FEX proteins during fluoride stress.</description><identifier>ISSN: 2190-572X</identifier><identifier>EISSN: 2190-5738</identifier><identifier>DOI: 10.1007/s13205-019-1629-4</identifier><identifier>PMID: 30800614</identifier><language>eng</language><publisher>Cham: Springer International Publishing</publisher><subject>Acetylation ; Agriculture ; Bioinformatics ; Biomaterials ; Biotechnology ; Cancer Research ; Chemistry ; Chemistry and Materials Science ; Conserved sequence ; Eukaryotes ; eukaryotic cells ; Flowers & plants ; Fluorides ; genes ; Homology ; Lipids ; methylation ; moieties ; Original ; Original Article ; Phosphorylation ; plasma membrane ; Post-translation ; post-translational modification ; prediction ; Prokaryotes ; prokaryotic cells ; Proteins ; Riboswitches ; RNA ; Stem Cells ; transporters ; xenobiotics</subject><ispartof>3 Biotech, 2019-03, Vol.9 (3), p.103-103, Article 103</ispartof><rights>King Abdulaziz City for Science and Technology 2019</rights><rights>King Abdulaziz City for Science and Technology 2019.</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c503t-c98586660fa7143579a772418d9b8247b153248eb40e61b33f3775e56817375e3</citedby><cites>FETCH-LOGICAL-c503t-c98586660fa7143579a772418d9b8247b153248eb40e61b33f3775e56817375e3</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktopdf>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6386761/pdf/$$EPDF$$P50$$Gpubmedcentral$$H</linktopdf><linktohtml>$$Uhttps://www.ncbi.nlm.nih.gov/pmc/articles/PMC6386761/$$EHTML$$P50$$Gpubmedcentral$$H</linktohtml><link.rule.ids>230,314,723,776,780,881,27901,27902,41464,42533,51294,53766,53768</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/30800614$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Banerjee, Aditya</creatorcontrib><creatorcontrib>Roychoudhury, Aryadeep</creatorcontrib><title>Structural introspection of a putative fluoride transporter in plants</title><title>3 Biotech</title><addtitle>3 Biotech</addtitle><addtitle>3 Biotech</addtitle><description>The xenobiotic fluoride is a detrimental toxin which is exported by a double-barrelled fluoride channel (Fluc) in prokaryotes and a single-barrelled fluoride exporter (FEX) in lower eukaryotes. The presence of
FEX
gene in higher plant species has not been reported till date. In this communication, we have identified FEXs across nine plant species belonging to five different families. Homology modelling predicted the sequential and structural conservation of crucial residues in plant FEXs. It was predicted that the N-terminal segments were the main target sites for phosphorylation. Other post-translational modifications included Arg methylation, Lys acetylation and Cys
S
-nitrosylation, all of which contribute to protein stability and function. FEXs were predicted to contain lipid moieties which anchor the transporters to the plasma membrane. The crystallizability along with associated properties of plant FEXs was also analyzed to facilitate future experimental analyses. The predicted RNA structure of
OsFEX
formed several pseudoknots, though no riboswitches could be detected from our prediction. The analysis of upstream regions of
FEX
in representative plants represented that this gene could be responsive to phytohormone-mediated signaling. This is the first novel report highlighting that
FEX
genes in plants are probably expressed in a tissue-specific pattern and possibly via a phytohormone-dependent pathway to encode functional FEX proteins during fluoride stress.</description><subject>Acetylation</subject><subject>Agriculture</subject><subject>Bioinformatics</subject><subject>Biomaterials</subject><subject>Biotechnology</subject><subject>Cancer Research</subject><subject>Chemistry</subject><subject>Chemistry and Materials Science</subject><subject>Conserved sequence</subject><subject>Eukaryotes</subject><subject>eukaryotic cells</subject><subject>Flowers & plants</subject><subject>Fluorides</subject><subject>genes</subject><subject>Homology</subject><subject>Lipids</subject><subject>methylation</subject><subject>moieties</subject><subject>Original</subject><subject>Original Article</subject><subject>Phosphorylation</subject><subject>plasma membrane</subject><subject>Post-translation</subject><subject>post-translational modification</subject><subject>prediction</subject><subject>Prokaryotes</subject><subject>prokaryotic cells</subject><subject>Proteins</subject><subject>Riboswitches</subject><subject>RNA</subject><subject>Stem Cells</subject><subject>transporters</subject><subject>xenobiotics</subject><issn>2190-572X</issn><issn>2190-5738</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2019</creationdate><recordtype>article</recordtype><recordid>eNqFkUtL9TAQhoMoKuoPcPNRcOOmmsm9G0HEGwguVHAX0p5UKz1NTVLBf-_I0eOnIGaTgXnmnctLyC7QA6BUHybgjMqSQlWCYlUpVsgmg4qWUnOzuozZ_QbZSemJ4pMgK6DrZINTQ6kCsUlOb3KcmjxF1xfdkGNIo29yF4YitIUrxim73L34ou2nELuZL3J0QxpDzD5iQTH2bshpm6y1rk9-5-PfIndnp7cnF-XV9fnlyfFV2UjKc9lURhqlFG2dBsGlrpzWTICZVbVhQtcgORPG14J6BTXnLddaeqkMaI4B3yJHC91xqud-1nic2PV2jN3cxVcbXGe_Z4bu0T6EF6u4UVoBCux_CMTwPPmU7bxLje9xCx-mZBljeFzFqPobBVxGC7QC0b0f6FOY4oCXsEwCVExLIZGCBdXglVP07XJuoPbdUruw1KKl9t1SK7Dm3_8LLys-DUSALYCEqeHBx6_Wv6u-AbhqqmI</recordid><startdate>20190301</startdate><enddate>20190301</enddate><creator>Banerjee, Aditya</creator><creator>Roychoudhury, Aryadeep</creator><general>Springer International Publishing</general><general>Springer Nature B.V</general><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope><scope>7X8</scope><scope>7S9</scope><scope>L.6</scope><scope>5PM</scope></search><sort><creationdate>20190301</creationdate><title>Structural introspection of a putative fluoride transporter in plants</title><author>Banerjee, Aditya ; Roychoudhury, Aryadeep</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c503t-c98586660fa7143579a772418d9b8247b153248eb40e61b33f3775e56817375e3</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2019</creationdate><topic>Acetylation</topic><topic>Agriculture</topic><topic>Bioinformatics</topic><topic>Biomaterials</topic><topic>Biotechnology</topic><topic>Cancer Research</topic><topic>Chemistry</topic><topic>Chemistry and Materials Science</topic><topic>Conserved sequence</topic><topic>Eukaryotes</topic><topic>eukaryotic cells</topic><topic>Flowers & plants</topic><topic>Fluorides</topic><topic>genes</topic><topic>Homology</topic><topic>Lipids</topic><topic>methylation</topic><topic>moieties</topic><topic>Original</topic><topic>Original Article</topic><topic>Phosphorylation</topic><topic>plasma membrane</topic><topic>Post-translation</topic><topic>post-translational modification</topic><topic>prediction</topic><topic>Prokaryotes</topic><topic>prokaryotic cells</topic><topic>Proteins</topic><topic>Riboswitches</topic><topic>RNA</topic><topic>Stem Cells</topic><topic>transporters</topic><topic>xenobiotics</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Banerjee, Aditya</creatorcontrib><creatorcontrib>Roychoudhury, Aryadeep</creatorcontrib><collection>PubMed</collection><collection>CrossRef</collection><collection>MEDLINE - Academic</collection><collection>AGRICOLA</collection><collection>AGRICOLA - Academic</collection><collection>PubMed Central (Full Participant titles)</collection><jtitle>3 Biotech</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Banerjee, Aditya</au><au>Roychoudhury, Aryadeep</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Structural introspection of a putative fluoride transporter in plants</atitle><jtitle>3 Biotech</jtitle><stitle>3 Biotech</stitle><addtitle>3 Biotech</addtitle><date>2019-03-01</date><risdate>2019</risdate><volume>9</volume><issue>3</issue><spage>103</spage><epage>103</epage><pages>103-103</pages><artnum>103</artnum><issn>2190-572X</issn><eissn>2190-5738</eissn><abstract>The xenobiotic fluoride is a detrimental toxin which is exported by a double-barrelled fluoride channel (Fluc) in prokaryotes and a single-barrelled fluoride exporter (FEX) in lower eukaryotes. The presence of
FEX
gene in higher plant species has not been reported till date. In this communication, we have identified FEXs across nine plant species belonging to five different families. Homology modelling predicted the sequential and structural conservation of crucial residues in plant FEXs. It was predicted that the N-terminal segments were the main target sites for phosphorylation. Other post-translational modifications included Arg methylation, Lys acetylation and Cys
S
-nitrosylation, all of which contribute to protein stability and function. FEXs were predicted to contain lipid moieties which anchor the transporters to the plasma membrane. The crystallizability along with associated properties of plant FEXs was also analyzed to facilitate future experimental analyses. The predicted RNA structure of
OsFEX
formed several pseudoknots, though no riboswitches could be detected from our prediction. The analysis of upstream regions of
FEX
in representative plants represented that this gene could be responsive to phytohormone-mediated signaling. This is the first novel report highlighting that
FEX
genes in plants are probably expressed in a tissue-specific pattern and possibly via a phytohormone-dependent pathway to encode functional FEX proteins during fluoride stress.</abstract><cop>Cham</cop><pub>Springer International Publishing</pub><pmid>30800614</pmid><doi>10.1007/s13205-019-1629-4</doi><tpages>1</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Acetylation Agriculture Bioinformatics Biomaterials Biotechnology Cancer Research Chemistry Chemistry and Materials Science Conserved sequence Eukaryotes eukaryotic cells Flowers & plants Fluorides genes Homology Lipids methylation moieties Original Original Article Phosphorylation plasma membrane Post-translation post-translational modification prediction Prokaryotes prokaryotic cells Proteins Riboswitches RNA Stem Cells transporters xenobiotics |
title | Structural introspection of a putative fluoride transporter in plants |
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