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
Hauptverfasser: Bienert, Gerd P, Cavez, Damien, Besserer, Arnaud, Berny, Marie C, Gilis, Dimitri, Rooman, Marianne, Chaumont, François
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container_end_page 111
container_issue 1
container_start_page 101
container_title Biochemical journal
container_volume 445
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
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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. 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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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