PEP3 overexpression shortens lag phase but does not alter growth rate in Saccharomyces cerevisiae exposed to acetic acid stress
| LEADER | caa a22 4500 | ||
|---|---|---|---|
| 001 | 605499632 | ||
| 003 | CHVBK | ||
| 005 | 20210128100552.0 | ||
| 007 | cr unu---uuuuu | ||
| 008 | 210128e20151001xx s 000 0 eng | ||
| 024 | 7 | 0 | |a 10.1007/s00253-015-6708-9 |2 doi |
| 035 | |a (NATIONALLICENCE)springer-10.1007/s00253-015-6708-9 | ||
| 245 | 0 | 0 | |a PEP3 overexpression shortens lag phase but does not alter growth rate in Saccharomyces cerevisiae exposed to acetic acid stress |h [Elektronische Daten] |c [Jun Ding, Garrett Holzwarth, C. Bradford, Ben Cooley, Allen Yoshinaga, Jana Patton-Vogt, Hagai Abeliovich, Michael Penner, Alan Bakalinsky] |
| 520 | 3 | |a In fungi, two recognized mechanisms contribute to pH homeostasis: the plasma membrane proton-pumping ATPase that exports excess protons and the vacuolar proton-pumping ATPase (V-ATPase) that mediates vacuolar proton uptake. Here, we report that overexpression of PEP3 which encodes a component of the HOPS and CORVET complexes involved in vacuolar biogenesis, shortened lag phase in Saccharomyces cerevisiae exposed to acetic acid stress. By confocal microscopy, PEP3-overexpressing cells stained with the vacuolar membrane-specific dye, FM4-64 had more fragmented vacuoles than the wild-type control. The stained overexpression mutant was also found to exhibit about 3.6-fold more FM4-64 fluorescence than the wild-type control as determined by flow cytometry. While the vacuolar pH of the wild-type strain grown in the presence of 80mM acetic acid was significantly higher than in the absence of added acid, no significant difference was observed in vacuolar pH of the overexpression strain grown either in the presence or absence of 80mM acetic acid. Based on an indirect growth assay, the PEP3-overexpression strain exhibited higher V-ATPase activity. We hypothesize that PEP3 overexpression provides protection from acid stress by increasing vacuolar surface area and V-ATPase activity and, hence, proton-sequestering capacity. | |
| 540 | |a Springer-Verlag Berlin Heidelberg, 2015 | ||
| 690 | 7 | |a Saccharomyces cerevisiae |2 nationallicence | |
| 690 | 7 | |a Yeast |2 nationallicence | |
| 690 | 7 | |a Acetic acid |2 nationallicence | |
| 690 | 7 | |a PEP3 |2 nationallicence | |
| 690 | 7 | |a V-ATPase |2 nationallicence | |
| 690 | 7 | |a HOPS |2 nationallicence | |
| 690 | 7 | |a CORVET |2 nationallicence | |
| 690 | 7 | |a Vacuole |2 nationallicence | |
| 690 | 7 | |a STM1 |2 nationallicence | |
| 690 | 7 | |a PEP5 |2 nationallicence | |
| 700 | 1 | |a Ding |D Jun |u Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA |4 aut | |
| 700 | 1 | |a Holzwarth |D Garrett |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | |
| 700 | 1 | |a Bradford |D C. |u Department of Environmental & Molecular Toxicology, Oregon State University, Corvallis, OR, USA |4 aut | |
| 700 | 1 | |a Cooley |D Ben |u Biological Sciences, Duquesne University, Pittsburgh, PA, USA |4 aut | |
| 700 | 1 | |a Yoshinaga |D Allen |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | |
| 700 | 1 | |a Patton-Vogt |D Jana |u Biological Sciences, Duquesne University, Pittsburgh, PA, USA |4 aut | |
| 700 | 1 | |a Abeliovich |D Hagai |u Department of Biochemistry and Food Science, Hebrew University, Rehovot, Israel |4 aut | |
| 700 | 1 | |a Penner |D Michael |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | |
| 700 | 1 | |a Bakalinsky |D Alan |u Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA |4 aut | |
| 773 | 0 | |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/20(2015-10-01), 8667-8680 |x 0175-7598 |q 99:20<8667 |1 2015 |2 99 |o 253 | |
| 856 | 4 | 0 | |u https://doi.org/10.1007/s00253-015-6708-9 |q text/html |z Onlinezugriff via DOI |
| 898 | |a BK010053 |b XK010053 |c XK010000 | ||
| 900 | 7 | |a Metadata rights reserved |b Springer special CC-BY-NC licence |2 nationallicence | |
| 908 | |D 1 |a research-article |2 jats | ||
| 949 | |B NATIONALLICENCE |F NATIONALLICENCE |b NL-springer | ||
| 950 | |B NATIONALLICENCE |P 856 |E 40 |u https://doi.org/10.1007/s00253-015-6708-9 |q text/html |z Onlinezugriff via DOI | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Ding |D Jun |u Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Holzwarth |D Garrett |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bradford |D C. |u Department of Environmental & Molecular Toxicology, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Cooley |D Ben |u Biological Sciences, Duquesne University, Pittsburgh, PA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Yoshinaga |D Allen |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Patton-Vogt |D Jana |u Biological Sciences, Duquesne University, Pittsburgh, PA, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Abeliovich |D Hagai |u Department of Biochemistry and Food Science, Hebrew University, Rehovot, Israel |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Penner |D Michael |u Department of Food Science and Technology, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 700 |E 1- |a Bakalinsky |D Alan |u Department of Biochemistry and Biophysics, Oregon State University, Corvallis, OR, USA |4 aut | ||
| 950 | |B NATIONALLICENCE |P 773 |E 0- |t Applied Microbiology and Biotechnology |d Springer Berlin Heidelberg |g 99/20(2015-10-01), 8667-8680 |x 0175-7598 |q 99:20<8667 |1 2015 |2 99 |o 253 | ||