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Plant Physiol Biochem. 2013 Sep;70:52-60. doi: 10.1016/j.plaphy.2013.05.015. Epub 2013 May 25.

The nucleobase cation symporter 1 of Chlamydomonas reinhardtii and that of the evolutionarily distant Arabidopsis thaliana display parallel function and establish a plant-specific solute transport profile.

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1
Department of Biology, Indiana University-Purdue University Fort Wayne, 2101 East Coliseum Blvd., Fort Wayne, IN 46805, USA. schejr02@ipfw.edu

Abstract

The single cell alga Chlamydomonas reinhardtii is capable of importing purines as nitrogen sources. An analysis of the annotated C. reinhardtii genome reveals at least three distinct gene families encoding for known nucleobase transporters. In this study the solute transport and binding properties for the lone C. reinhardtii nucleobase cation symporter 1 (CrNCS1) are determined through heterologous expression in Saccharomyces cerevisiae. CrNCS1 acts as a transporter of adenine, guanine, uracil and allantoin, sharing similar - but not identical - solute recognition specificity with the evolutionary distant NCS1 from Arabidopsis thaliana. The results suggest that the solute specificity for plant NCS1 occurred early in plant evolution and are distinct from solute transport specificities of single cell fungal NCS1 proteins.

KEYWORDS:

Chlamydomonas; Nucleobase cation symporter 1; Purine; Pyrimidine; Transport

PMID:
23770594
DOI:
10.1016/j.plaphy.2013.05.015
[Indexed for MEDLINE]
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