A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers
AQPs (aquaporins) are conserved in all kingdoms of life and facilitate the rapid diffusion of water and/or other small solutes across cell membranes. Among the different plant AQPs, PIPs (plasma membrane intrinsic proteins), which fall into two phylogenetic groups, PIP1 and PIP2, play key roles in p...
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Veröffentlicht in: | Biochemical journal 2012-07, Vol.445 (1), p.101-111 |
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creator | Bienert, Gerd P Cavez, Damien Besserer, Arnaud Berny, Marie C Gilis, Dimitri Rooman, Marianne Chaumont, François |
description | AQPs (aquaporins) are conserved in all kingdoms of life and facilitate the rapid diffusion of water and/or other small solutes across cell membranes. Among the different plant AQPs, PIPs (plasma membrane intrinsic proteins), which fall into two phylogenetic groups, PIP1 and PIP2, play key roles in plant water transport processes. PIPs form tetramers in which each monomer acts as a functional channel. The intermolecular interactions that stabilize PIP oligomer complexes and are responsible for the resistance of PIP dimers to denaturating conditions are not well characterized. In the present study, we identified a highly conserved cysteine residue in loop A of PIP1 and PIP2 proteins and demonstrated by mutagenesis that it is involved in the formation of a disulfide bond between two monomers. Although this cysteine seems not to be involved in regulation of trafficking to the plasma membrane, activity, substrate selectivity or oxidative gating of ZmPIP1s (Zm is Zea mays), ZmPIP2s and hetero-oligomers, it increases oligomer stability under denaturating conditions. In addition, when PIP1 and PIP2 are co-expressed, the loop A cysteine of ZmPIP1;2, but not that of ZmPIP2;5, is involved in the mercury sensitivity of the channels. |
doi_str_mv | 10.1042/bj20111704 |
format | Article |
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Among the different plant AQPs, PIPs (plasma membrane intrinsic proteins), which fall into two phylogenetic groups, PIP1 and PIP2, play key roles in plant water transport processes. PIPs form tetramers in which each monomer acts as a functional channel. The intermolecular interactions that stabilize PIP oligomer complexes and are responsible for the resistance of PIP dimers to denaturating conditions are not well characterized. In the present study, we identified a highly conserved cysteine residue in loop A of PIP1 and PIP2 proteins and demonstrated by mutagenesis that it is involved in the formation of a disulfide bond between two monomers. Although this cysteine seems not to be involved in regulation of trafficking to the plasma membrane, activity, substrate selectivity or oxidative gating of ZmPIP1s (Zm is Zea mays), ZmPIP2s and hetero-oligomers, it increases oligomer stability under denaturating conditions. In addition, when PIP1 and PIP2 are co-expressed, the loop A cysteine of ZmPIP1;2, but not that of ZmPIP2;5, is involved in the mercury sensitivity of the channels.</description><identifier>ISSN: 0264-6021</identifier><identifier>EISSN: 1470-8728</identifier><identifier>DOI: 10.1042/bj20111704</identifier><identifier>PMID: 22506965</identifier><language>eng</language><publisher>England</publisher><subject>Amino Acid Sequence ; Animals ; Aquaporins - genetics ; Aquaporins - metabolism ; Biological Transport ; Blotting, Western ; Cell Membrane - metabolism ; Cysteine - chemistry ; Cysteine - metabolism ; Disulfides - metabolism ; Female ; Gene Expression Regulation, Plant ; Molecular Sequence Data ; Oocytes - cytology ; Oocytes - metabolism ; Plant Proteins - genetics ; Plant Proteins - metabolism ; Protein Biosynthesis ; Protein Conformation ; Protein Folding ; Protein Multimerization ; RNA, Messenger - genetics ; Sequence Homology, Amino Acid ; Water - metabolism ; Xenopus laevis ; Zea mays - genetics ; Zea mays - growth & development ; Zea mays - metabolism</subject><ispartof>Biochemical journal, 2012-07, Vol.445 (1), p.101-111</ispartof><lds50>peer_reviewed</lds50><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c394t-8c6026b388e7e31b89a13a1803e0d175c18b885d67be0702f215a040c72560a73</citedby><cites>FETCH-LOGICAL-c394t-8c6026b388e7e31b89a13a1803e0d175c18b885d67be0702f215a040c72560a73</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,27924,27925</link.rule.ids><backlink>$$Uhttps://www.ncbi.nlm.nih.gov/pubmed/22506965$$D View this record in MEDLINE/PubMed$$Hfree_for_read</backlink></links><search><creatorcontrib>Bienert, Gerd P</creatorcontrib><creatorcontrib>Cavez, Damien</creatorcontrib><creatorcontrib>Besserer, Arnaud</creatorcontrib><creatorcontrib>Berny, Marie C</creatorcontrib><creatorcontrib>Gilis, Dimitri</creatorcontrib><creatorcontrib>Rooman, Marianne</creatorcontrib><creatorcontrib>Chaumont, François</creatorcontrib><title>A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers</title><title>Biochemical journal</title><addtitle>Biochem J</addtitle><description>AQPs (aquaporins) are conserved in all kingdoms of life and facilitate the rapid diffusion of water and/or other small solutes across cell membranes. Among the different plant AQPs, PIPs (plasma membrane intrinsic proteins), which fall into two phylogenetic groups, PIP1 and PIP2, play key roles in plant water transport processes. PIPs form tetramers in which each monomer acts as a functional channel. The intermolecular interactions that stabilize PIP oligomer complexes and are responsible for the resistance of PIP dimers to denaturating conditions are not well characterized. In the present study, we identified a highly conserved cysteine residue in loop A of PIP1 and PIP2 proteins and demonstrated by mutagenesis that it is involved in the formation of a disulfide bond between two monomers. Although this cysteine seems not to be involved in regulation of trafficking to the plasma membrane, activity, substrate selectivity or oxidative gating of ZmPIP1s (Zm is Zea mays), ZmPIP2s and hetero-oligomers, it increases oligomer stability under denaturating conditions. In addition, when PIP1 and PIP2 are co-expressed, the loop A cysteine of ZmPIP1;2, but not that of ZmPIP2;5, is involved in the mercury sensitivity of the channels.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Aquaporins - genetics</subject><subject>Aquaporins - metabolism</subject><subject>Biological Transport</subject><subject>Blotting, Western</subject><subject>Cell Membrane - metabolism</subject><subject>Cysteine - chemistry</subject><subject>Cysteine - metabolism</subject><subject>Disulfides - metabolism</subject><subject>Female</subject><subject>Gene Expression Regulation, Plant</subject><subject>Molecular Sequence Data</subject><subject>Oocytes - cytology</subject><subject>Oocytes - metabolism</subject><subject>Plant Proteins - genetics</subject><subject>Plant Proteins - metabolism</subject><subject>Protein Biosynthesis</subject><subject>Protein Conformation</subject><subject>Protein Folding</subject><subject>Protein Multimerization</subject><subject>RNA, Messenger - genetics</subject><subject>Sequence Homology, Amino Acid</subject><subject>Water - metabolism</subject><subject>Xenopus laevis</subject><subject>Zea mays - genetics</subject><subject>Zea mays - growth & development</subject><subject>Zea mays - metabolism</subject><issn>0264-6021</issn><issn>1470-8728</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2012</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNo9kMtOwzAQRS0EoqWw4QOQ10iBsfOwuywVT1ViA-vIjieSq9gOdlLE35OqlM3cxRwdzVxCrhncMSj4vd5yYIwJKE7InBUCMim4PCVz4FWRVcDZjFyktAVgBRRwTmacl1Atq3JOxhVtgk8Yd2ho85MGtB5pxGTNiNQmav0udPul9dTYNHatNUh18Ia2ITo12OCpxuEb0dO-U37Yz-QUdeh0VJNNfY2qD3ESuOCDw5guyVmruoRXf7kgn0-PH-uXbPP-_LpebbImXxZDJpvp-ErnUqLAnGm5VCxXTEKOYJgoGya1lKWphEYQwFvOSjV92AheVqBEviC3B28TQ0oR27qP1qn4UzOo993VD2_H7ib45gD3o3Zo_tFjWfkvXuRqnw</recordid><startdate>20120701</startdate><enddate>20120701</enddate><creator>Bienert, Gerd P</creator><creator>Cavez, Damien</creator><creator>Besserer, Arnaud</creator><creator>Berny, Marie C</creator><creator>Gilis, Dimitri</creator><creator>Rooman, Marianne</creator><creator>Chaumont, François</creator><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20120701</creationdate><title>A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers</title><author>Bienert, Gerd P ; Cavez, Damien ; Besserer, Arnaud ; Berny, Marie C ; Gilis, Dimitri ; Rooman, Marianne ; Chaumont, François</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c394t-8c6026b388e7e31b89a13a1803e0d175c18b885d67be0702f215a040c72560a73</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2012</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Aquaporins - genetics</topic><topic>Aquaporins - metabolism</topic><topic>Biological Transport</topic><topic>Blotting, Western</topic><topic>Cell Membrane - metabolism</topic><topic>Cysteine - chemistry</topic><topic>Cysteine - metabolism</topic><topic>Disulfides - metabolism</topic><topic>Female</topic><topic>Gene Expression Regulation, Plant</topic><topic>Molecular Sequence Data</topic><topic>Oocytes - cytology</topic><topic>Oocytes - metabolism</topic><topic>Plant Proteins - genetics</topic><topic>Plant Proteins - metabolism</topic><topic>Protein Biosynthesis</topic><topic>Protein Conformation</topic><topic>Protein Folding</topic><topic>Protein Multimerization</topic><topic>RNA, Messenger - genetics</topic><topic>Sequence Homology, Amino Acid</topic><topic>Water - metabolism</topic><topic>Xenopus laevis</topic><topic>Zea mays - genetics</topic><topic>Zea mays - growth & development</topic><topic>Zea mays - metabolism</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Bienert, Gerd P</creatorcontrib><creatorcontrib>Cavez, Damien</creatorcontrib><creatorcontrib>Besserer, Arnaud</creatorcontrib><creatorcontrib>Berny, Marie C</creatorcontrib><creatorcontrib>Gilis, Dimitri</creatorcontrib><creatorcontrib>Rooman, Marianne</creatorcontrib><creatorcontrib>Chaumont, François</creatorcontrib><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>Biochemical journal</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Bienert, Gerd P</au><au>Cavez, Damien</au><au>Besserer, Arnaud</au><au>Berny, Marie C</au><au>Gilis, Dimitri</au><au>Rooman, Marianne</au><au>Chaumont, François</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers</atitle><jtitle>Biochemical journal</jtitle><addtitle>Biochem J</addtitle><date>2012-07-01</date><risdate>2012</risdate><volume>445</volume><issue>1</issue><spage>101</spage><epage>111</epage><pages>101-111</pages><issn>0264-6021</issn><eissn>1470-8728</eissn><abstract>AQPs (aquaporins) are conserved in all kingdoms of life and facilitate the rapid diffusion of water and/or other small solutes across cell membranes. Among the different plant AQPs, PIPs (plasma membrane intrinsic proteins), which fall into two phylogenetic groups, PIP1 and PIP2, play key roles in plant water transport processes. PIPs form tetramers in which each monomer acts as a functional channel. The intermolecular interactions that stabilize PIP oligomer complexes and are responsible for the resistance of PIP dimers to denaturating conditions are not well characterized. In the present study, we identified a highly conserved cysteine residue in loop A of PIP1 and PIP2 proteins and demonstrated by mutagenesis that it is involved in the formation of a disulfide bond between two monomers. Although this cysteine seems not to be involved in regulation of trafficking to the plasma membrane, activity, substrate selectivity or oxidative gating of ZmPIP1s (Zm is Zea mays), ZmPIP2s and hetero-oligomers, it increases oligomer stability under denaturating conditions. In addition, when PIP1 and PIP2 are co-expressed, the loop A cysteine of ZmPIP1;2, but not that of ZmPIP2;5, is involved in the mercury sensitivity of the channels.</abstract><cop>England</cop><pmid>22506965</pmid><doi>10.1042/bj20111704</doi><tpages>11</tpages></addata></record> |
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source | MEDLINE; Elektronische Zeitschriftenbibliothek - Frei zugängliche E-Journals; PubMed Central |
subjects | Amino Acid Sequence Animals Aquaporins - genetics Aquaporins - metabolism Biological Transport Blotting, Western Cell Membrane - metabolism Cysteine - chemistry Cysteine - metabolism Disulfides - metabolism Female Gene Expression Regulation, Plant Molecular Sequence Data Oocytes - cytology Oocytes - metabolism Plant Proteins - genetics Plant Proteins - metabolism Protein Biosynthesis Protein Conformation Protein Folding Protein Multimerization RNA, Messenger - genetics Sequence Homology, Amino Acid Water - metabolism Xenopus laevis Zea mays - genetics Zea mays - growth & development Zea mays - metabolism |
title | A conserved cysteine residue is involved in disulfide bond formation between plant plasma membrane aquaporin monomers |
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