Heterologous complementation studies reveal the solute transport profiles of a two-member nucleobase cation symporter 1 (NCS1) family in Physcomitrella patens
Copyright © 2015 Elsevier Masson SAS. All rights reserved.
Veröffentlicht in: | Plant physiology and biochemistry : PPB. - 1991. - 100(2016) vom: 20. März, Seite 12-17 |
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1. Verfasser: | |
Weitere Verfasser: | , , , |
Format: | Online-Aufsatz |
Sprache: | English |
Veröffentlicht: |
2016
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Zugriff auf das übergeordnete Werk: | Plant physiology and biochemistry : PPB |
Schlagworte: | Journal Article Research Support, Non-U.S. Gov't Nucleobase cation symporter 1 Physcomitrella patens Purine and pyrimidine Transport Nucleobase Transport Proteins Plant Proteins |
Zusammenfassung: | Copyright © 2015 Elsevier Masson SAS. All rights reserved. As part of an evolution-function analysis, two nucleobase cation symporter 1 (NCS1) from the moss Physcomitrella patens (PpNCS1A and PpNCS1B) are examined--the first such analysis of nucleobase transporters from early land plants. The solute specificity profiles for the moss NCS1 were determined through heterologous expression, growth and radiolabeled uptake experiments in NCS1-deficient Saccharomyces cerevisiae. Both PpNCS1A and 1B, share the same profiles as high affinity transporters of adenine and transport uracil, guanine, 8-azaguanine, 8-azaadenine, cytosine, 5-fluorocytosine, hypoxanthine, and xanthine. Despite sharing the same solute specificity profile, PpNCS1A and PpNCS1B move nucleobase compounds with different efficiencies. The broad nucleobase transport profile of PpNCS1A and 1B differs from the recently-characterized Viridiplantae NCS1 in breadth, revealing a flexibility in solute interactions with NCS1 across plant evolution |
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Beschreibung: | Date Completed 10.11.2016 Date Revised 30.09.2020 published: Print-Electronic Citation Status MEDLINE |
ISSN: | 1873-2690 |
DOI: | 10.1016/j.plaphy.2015.12.014 |