Functional Assessment of the Medicago truncatula NIP/LATD Protein Demonstrates That It Is a High-Affinity Nitrate Transporter Metadata
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- Main Title Functional Assessment of the Medicago truncatula NIP/LATD Protein Demonstrates That It Is a High-Affinity Nitrate Transporter
Author: Bagchi, RammyaniCreator Type: PersonalCreator Info: University of North Texas
Author: Salehin, MohammadCreator Type: PersonalCreator Info: University of North Texas
Author: Adeyemo, O. SarahCreator Type: PersonalCreator Info: University of North Texas
Author: Salazar, CarolinaCreator Type: PersonalCreator Info: University of North Texas
Author: Shulaev, VladimirCreator Type: PersonalCreator Info: University of North Texas
Author: Sherrier, D. JanineCreator Type: PersonalCreator Info: University of Delaware
Author: Dickstein, RebeccaCreator Type: PersonalCreator Info: University of North Texas
Name: American Society of Plant BiologistsPlace of Publication: [Rockville, Maryland]
- Creation: 2012-10
- Content Description: Article on the functional assessment of the Medicago truncatula NIP/LATD protein demonstrating that it is a high-affinity nitrate transporter.
- Physical Description: 11 p.
- Keyword: genes
- Keyword: proteins
- Keyword: medicago truncatula
- Keyword: nitrogen
- Journal: Plant Physiology, 2012, Rockville: American Society of Plant Biologists, pp. 906-916
- Publication Title: Plant Physiology
- Volume: 160
- Issue: 2
- Page Start: 906
- Page End: 916
- Peer Reviewed: True
Name: UNT Scholarly WorksCode: UNTSW
Name: UNT College of Arts and SciencesCode: UNTCAS
- Rights Access: public
- DOI: 10.1104/pp.112.196444
- Archival Resource Key: ark:/67531/metadc130185
- Academic Department: Biological Sciences
- Display Note: Plant Physiology, October 2012, Vol. 160, pp. 906-916, www.plantphysiol.org; © American Society of Plant Physiologists.
- Display Note: Abstract: The Medicago truncatula NIP/LATD (for Numerous Infections and Polyphenolics/Lateral root-organ Defective) gene encodes a protein found in a clade of nitrate transporters within the large NRT1(PTR) family that also encodes transporters of dipeptides and tripeptides, dicarboxylates, auxin, and abscisic acid. Of the NRT1(PTR) members known to transport nitrate, most are low-affinity transporters. Here, the authors show that M. truncatula nip/latd mutants are more defective in their lateral root responses to nitrate provided at low (250 μм) concentrations than at higher (5mм) concentrations; however, nitrate uptake experiments showed no discernible differences in uptake in the mutants. Heterologous expression experiments showed that MtNIP/LATD encodes a nitrate transporter: expression in Xenopus laevis oocytes conferred upon the oocytes the ability to take up nitrate from the medium, but oocytes expressing the less severe Mtnip-3 allele were proficient in nitrate transport. M. truncatula nip/latd mutants have pleiotropic defects in nodulation and root architecture defects but not for nodulation defects. This suggests that the spectrum of activities inherent in AtNRT1.1 is different from that possessed by MtNIP/LATD, but it could also reflect stability differences of each protein in M. truncatula. Collectively, the data show that MtNIP/LATD is a high-affinity nitrate transporter and suggest that it could have another function.