Limits...
A new pma1 mutation identified in a chronologically long-lived fission yeast mutant.

Naito C, Ito H, Oshiro T, Ohtsuka H, Murakami H, Aiba H - FEBS Open Bio (2014)

Bottom Line: We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase.An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast.This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Molecular Microbiology, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.

ABSTRACT
We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase. An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast. This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1.

No MeSH data available.


Glucose consumption. Cells were grown in SD medium at 30 °C, and the glucose concentrations in medium with wild type (open triangles) and L16 mutant (closed triangles) cells were determined. Wild type (open circles) and L16 mutant (closed circles) cell growth was monitored at OD600. Experiments were duplicated, with similar results. The representative data are shown.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
getmorefigures.php?uid=PMC4219986&req=5

f0025: Glucose consumption. Cells were grown in SD medium at 30 °C, and the glucose concentrations in medium with wild type (open triangles) and L16 mutant (closed triangles) cells were determined. Wild type (open circles) and L16 mutant (closed circles) cell growth was monitored at OD600. Experiments were duplicated, with similar results. The representative data are shown.

Mentions: Pma1 H+-ATPase is involved in H+-dependent nutrient uptake [14]. Pma1 ATPase functions physiologically to pump protons out of a cell, thus generating an electrochemical gradient that drives solute uptake by an array of H+-coupled co-transporters. In S. pombe, glucose uptake is energy dependent and is driven by the plasma membrane ATPase-generated electrochemical gradient [15]. We compared glucose consumption during growth between wild-type and L16 mutant cells (Fig. 5). This revealed that the L16 mutant consumed less glucose compared with wild type cells. This difference in glucose consumption was likely due to the differences in Pma1 activity that provides the proton gradient for glucose uptake.


A new pma1 mutation identified in a chronologically long-lived fission yeast mutant.

Naito C, Ito H, Oshiro T, Ohtsuka H, Murakami H, Aiba H - FEBS Open Bio (2014)

Glucose consumption. Cells were grown in SD medium at 30 °C, and the glucose concentrations in medium with wild type (open triangles) and L16 mutant (closed triangles) cells were determined. Wild type (open circles) and L16 mutant (closed circles) cell growth was monitored at OD600. Experiments were duplicated, with similar results. The representative data are shown.
© Copyright Policy - CC BY-NC-ND
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC4219986&req=5

f0025: Glucose consumption. Cells were grown in SD medium at 30 °C, and the glucose concentrations in medium with wild type (open triangles) and L16 mutant (closed triangles) cells were determined. Wild type (open circles) and L16 mutant (closed circles) cell growth was monitored at OD600. Experiments were duplicated, with similar results. The representative data are shown.
Mentions: Pma1 H+-ATPase is involved in H+-dependent nutrient uptake [14]. Pma1 ATPase functions physiologically to pump protons out of a cell, thus generating an electrochemical gradient that drives solute uptake by an array of H+-coupled co-transporters. In S. pombe, glucose uptake is energy dependent and is driven by the plasma membrane ATPase-generated electrochemical gradient [15]. We compared glucose consumption during growth between wild-type and L16 mutant cells (Fig. 5). This revealed that the L16 mutant consumed less glucose compared with wild type cells. This difference in glucose consumption was likely due to the differences in Pma1 activity that provides the proton gradient for glucose uptake.

Bottom Line: We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase.An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast.This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1.

View Article: PubMed Central - PubMed

Affiliation: Laboratory of Molecular Microbiology, Graduate School of Bioagricultural Sciences, Nagoya University, Chikusa-ku, Nagoya 464-8601, Japan.

ABSTRACT
We isolated a chronologically long-lived mutant of Schizosaccharomyces pombe and found a new mutation in pma1 (+) that encoded for an essential P-type proton ATPase. An Asp-138 to Asn mutation resulted in reduced Pma1 activity, concomitant with an increase in the chronological lifespan of this fission yeast. This study corroborates our previous report indicating Pma1 activity is crucial for the determination of life span of fission yeast, and offers information for better understanding of the enzyme, Pma1.

No MeSH data available.