Functional Assessment of the Medicago truncatula NIP/LATD Protein Demonstrates That It Is a High-Affinity Nitrate Transporter

Description:

Article on the functional assessment of the Medicago truncatula NIP/LATD protein demonstrating that it is a high-affinity nitrate transporter.

Creator(s):
Creation Date: October 2012
Partner(s):
UNT College of Arts and Sciences
Collection(s):
UNT Scholarly Works
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Creator (Author):
Bagchi, Rammyani

University of North Texas

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Salehin, Mohammad

University of North Texas

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Adeyemo, O. Sarah

University of North Texas

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Salazar, Carolina

University of North Texas

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Shulaev, Vladimir

University of North Texas

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Sherrier, D. Janine

University of Delaware

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Dickstein, Rebecca

University of North Texas

Publisher Info:
Place of Publication: [Rockville, Maryland]
Date(s):
  • Creation: October 2012
Description:

Article on the functional assessment of the Medicago truncatula NIP/LATD protein demonstrating that it is a high-affinity nitrate transporter.

Degree:
Department: Biological Sciences
Note:

Plant Physiology, October 2012, Vol. 160, pp. 906-916, www.plantphysiol.org; © American Society of Plant Physiologists.

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.

Physical Description:

11 p.

Language(s):
Subject(s):
Keyword(s): genes | proteins | medicago truncatula | nitrogen
Source: Plant Physiology, 2012, Rockville: American Society of Plant Biologists, pp. 906-916
Partner:
UNT College of Arts and Sciences
Collection:
UNT Scholarly Works
Identifier:
  • DOI: 10.1104/pp.112.196444
  • ARK: ark:/67531/metadc130185
Resource Type: Article
Format: Text
Rights:
Access: Public
Citation:
Publication Title: Plant Physiology
Volume: 160
Issue: 2
Page Start: 906
Page End: 916
Peer Reviewed: Yes