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https://hdl.handle.net/2440/70399
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dc.contributor.author | Drew, D. | - |
dc.contributor.author | Hrmova, M. | - |
dc.contributor.author | Lunde, C. | - |
dc.contributor.author | Jacobs, A. | - |
dc.contributor.author | Tester, M. | - |
dc.contributor.author | Fincher, G. | - |
dc.date.issued | 2011 | - |
dc.identifier.citation | BBA: Biomembranes, 2011; 1808(6):1483-1492 | - |
dc.identifier.issn | 0005-2736 | - |
dc.identifier.issn | 1879-2642 | - |
dc.identifier.uri | http://hdl.handle.net/2440/70399 | - |
dc.description.abstract | PpENA1 is a membrane-spanning transporter from the moss Physcomitrella patens, and is the first type IID P-type ATPase to be reported in the plant kingdom. In Physcomitrella, PpENA1 is essential for normal growth under moderate salt stress, while in yeast, type IID ATPases provide a vital efflux mechanism for cells under high salt conditions by selectively transporting Na+ or K+ across the plasma membrane. To investigate the structural basis for cation-binding within the type IID ATPase subfamily, we used homology modeling to identify a highly conserved cation-binding pocket between membrane helix (MH) 4 and MH 6 of the membrane-spanning pore of PpENA1. Mutation of specific charged and polar residues on MHs 4-6 resulted in a decrease or loss of protein activity as measured by complementation assays in yeast. The E298S mutation on MH 4 of PpENA1 had the most significant effect on activity despite the presence of a serine at this position in fungal type IID ATPases. Activity was partially restored in an inactivated PpENA1 mutant by the insertion of two additional serine residues on MH 4 and one on MH 6 based on the presence of these residues in fungal type IID ATPases. Our results suggest that the residues responsible for cation-binding in PpENA1 are distinct from those in fungal type IID ATPases, and that a fungal-type cation binding site can be successfully engineered into the moss protein. | - |
dc.description.statementofresponsibility | Damian P. Drew, Maria Hrmova, Christina Lunde, Andrew K. Jacobs, Mark Tester and Geoffrey B. Fincher | - |
dc.language.iso | en | - |
dc.publisher | Elsevier Science BV | - |
dc.rights | © 2010 Elsevier B.V. All rights reserved. | - |
dc.source.uri | http://dx.doi.org/10.1016/j.bbamem.2010.11.013 | - |
dc.subject | Fungi | - |
dc.subject | Saccharomyces cerevisiae | - |
dc.subject | Bryopsida | - |
dc.subject | Cations | - |
dc.subject | Potassium | - |
dc.subject | Sodium | - |
dc.subject | Fungal Proteins | - |
dc.subject | Plant Proteins | - |
dc.subject | Immunoblotting | - |
dc.subject | Genetic Complementation Test | - |
dc.subject | Amino Acid Substitution | - |
dc.subject | Binding Sites | - |
dc.subject | Ion Transport | - |
dc.subject | Amino Acid Sequence | - |
dc.subject | Protein Structure, Secondary | - |
dc.subject | Protein Structure, Tertiary | - |
dc.subject | Protein Binding | - |
dc.subject | Sequence Homology, Amino Acid | - |
dc.subject | Mutation | - |
dc.subject | Models, Molecular | - |
dc.subject | Molecular Sequence Data | - |
dc.subject | Sodium-Potassium-Exchanging ATPase | - |
dc.title | Structural and functional analyses of PpENA1 provide insights into cation binding by type IID P-type ATPases in lower plants and fungi | - |
dc.type | Journal article | - |
dc.identifier.doi | 10.1016/j.bbamem.2010.11.013 | - |
dc.relation.grant | ARC | - |
pubs.publication-status | Published | - |
dc.identifier.orcid | Hrmova, M. [0000-0002-3545-0605] | - |
Appears in Collections: | Agriculture, Food and Wine publications Aurora harvest |
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