A single nucleotide change in theMNR1 (VCX1/HUM1) gene determines resistance to manganese inSaccharomyces cerevisiae

Pozo, Lourdes Del; Osaba, Lourdes; Corchero, Javier; Jiménez, Antonio Moreno

doi:10.1002/(sici)1097-0061(19990330)15:5<371::aid-yea380>3.0.co;2-p

Cited by 19 publications

(18 citation statements)

References 22 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The ability to alter substrate specificity of CAXs has also been demonstrated with yeast VCX1. VCX1 has a single nucleotide polymorphism (SNP) variant termed MNR1 that shows a Mn 2+ -tolerant phenotype (del Pozo et al, 1999;, reminiscent of the wide substrate range of plant CAXs.…”

Section: Structure and Function Of Plant Caxsmentioning

confidence: 99%

Diverse Functions and Molecular Properties Emerging for CAX Cation/H+ Exchangers in Plants

2006

View full text Add to dashboard Cite

Steep concentration gradients of many ions are actively maintained, with lower concentrations typically located in the cytosol, and higher concentrations in organelles and outside the cell. The vacuole is an important storage organelle for many ions. The concentration gradient of cations is established across the plant tonoplast, in part, by high-capacity cation/H+ (CAX) exchange activity. While plants may not be green yeast, analysis of CAX regulation and substrate specificity has been greatly aided by utilizing yeast as an experimental tool. The basic CAX biology in ARABIDOPSIS has immediate relevance toward understanding the functional interplay between diverse transport processes. The long-range applied goals are to identify novel transporters and express them in crop plants in order to "mine" nutrients out of the soil and into plants. In doing so, this could boost the levels of essential nutrients in plants.

show abstract

Section: Structure and Function Of Plant Caxsmentioning

confidence: 99%

Diverse Functions and Molecular Properties Emerging for CAX Cation/H+ Exchangers in Plants

2006

View full text Add to dashboard Cite

show abstract

“…For example, a spontaneous mutant yeast strain, due to a point mutation in the yeast Ca 2ϩ /H ϩ exchanger VCX1, has increased Mn 2ϩ resistance compared with wild type yeast (38). However, no ion competition studies or direct Mn 2ϩ transport measurements have been done on the native or mutated forms of the transporter.…”

Section: Specificity Of Plant Mnmentioning

confidence: 99%

Manganese Specificity Determinants in the ArabidopsisMetal/H+ Antiporter CAX2

Shigaki

Pittman

Hirschi

2003

Journal of Biological Chemistry

104

107

View full text Add to dashboard Cite

In plants and fungi, vacuolar transporters help remove potentially toxic cations from the cytosol. Metal/H؉ antiporters are involved in metal sequestration into the vacuole. However, the specific transport properties and the ability to manipulate these transporters to alter substrate specificity are poorly understood. The Arabidopsis thaliana cation exchangers, CAX1 and CAX2, can both transport Ca 2؉ into the vacuole. There are 11 CAX-like transporters in Arabidopsis; however, CAX2 was the only characterized CAX transporter capable of vacuolar Mn 2؉ transport when expressed in yeast. To determine the domains within CAX2 that mediate Mn 2؉ specificity, six CAX2 mutants were constructed that contained different regions of the CAX1 transporter. One class displayed no alterations in Mn 2؉ or Ca 2؉ transport, the second class showed a reduction in Ca 2؉ transport and no measurable Mn 2؉ transport, and the third mutant, which contained a 10-amino acid domain from CAX1 (CAX2-C), showed no reduction in Ca 2؉ transport and a complete loss of Mn 2؉ transport. The subdomain analysis of CAX2-C identified a 3-amino acid region that is responsible for Mn 2؉ specificity of CAX2. This study provides evidence for the feasibility of altering substrate specificity in a metal/H ؉ antiporter, an important family of transporters found in a variety of organisms.

show abstract

“…A glycine to alanine change in the C-terminal membrane-spanning domain may modify H ϩ /Ca 2ϩ transport (8). In another study, a point mutation in a central membrane-spanning domain has been implicated in altering the Mn 2ϩ transport of VCX1 (11). In sum, these findings only hint at structural motifs involved in H ϩ /cation specificity.…”

mentioning

confidence: 96%

Structural Determinants of Ca2+ Transport in the Arabidopsis H+/Ca2+Antiporter CAX1

Shigaki¹,

Cheng²,

Pittman³

et al. 2001

Journal of Biological Chemistry

View full text Add to dashboard Cite

Ca2؉ levels in plants, fungi, and bacteria are controlled in part by H ؉ /Ca 2؉ exchangers; however, the relationship between primary sequence and biological activity of these transporters has not been reported. transport mutants if a nine-amino acid region of CAX1 was inserted into CAX3 (CAX3-9). Biochemical analysis in yeast showed CAX3-9 had 36% of the H؉ /Ca 2؉ exchange activity as compared with CAX1; however, CAX3-9 and CAX1 appear to differ in their transport of other ions. Exchanging the nine-amino acid region of CAX1 into CAX2 doubled yeast vacuolar Ca 2؉ transport but did not appear to alter the transport of other ions. This nine-amino acid region is highly variable among the plant CAX-like transporters. These findings suggest that this region is involved in CAX-mediated Ca 2؉ specificity.

show abstract

A single nucleotide change in theMNR1 (VCX1/HUM1) gene determines resistance to manganese inSaccharomyces cerevisiae

Cited by 19 publications

References 22 publications

Diverse Functions and Molecular Properties Emerging for CAX Cation/H+ Exchangers in Plants

Diverse Functions and Molecular Properties Emerging for CAX Cation/H+ Exchangers in Plants

Manganese Specificity Determinants in the ArabidopsisMetal/H+ Antiporter CAX2

Structural Determinants of Ca2+ Transport in the Arabidopsis H+/Ca2+Antiporter CAX1

Contact Info

Product

Resources

About