TY - JOUR
T1 - The basidiomycete Ustilago maydis has two plasma membrane H +-ATPases related to fungi and plants
AU - Robles-Martínez, Leobarda
AU - Pardo, Juan Pablo
AU - Miranda, Manuel
AU - Mendez, Tavis L.
AU - Matus-Ortega, Macario Genaro
AU - Mendoza-Hernández, Guillermo
AU - Guerra-Sánchez, Guadalupe
N1 - Funding Information:
Acknowledgments This work was supported by grants from CGPI-IPN (2010, 2011, and 2012), Consejo Nacional de Ciencia y Tecnología (CONACyT 59855) and Programa de Apoyo a Proyectos de Investiga-ción e Innovación Tecnológica (PAPIIT IN219107-3), Universidad Nacional Autónoma de México (UNAM). This work is part of the Ph.D. studies of Robles-Martínez L in the Doctorado de Ciencias Quimicobiológicas, Instituto Politécnico Nacional. She is receiving a doctoral fellowship Grants from CONACyT (2009–2013) and PIFI-IPN (2009–2013). This study was partly supported by grant NIMH 5SC1MH 086070-04 to MM and also in part by the grant 8G12MD007592 to the Border Biomedical Research Center (BBRC)/University of Texas at El Paso) from the National Institute on Minority Health Disparities (NIHMD).
PY - 2013/10
Y1 - 2013/10
N2 - The fungal and plant plasma membrane H+-ATPases play critical roles in the physiology of yeast, plant and protozoa cells. We identified two genes encoding two plasma membrane H+-ATPases in the basidiomycete Ustilago maydis, one protein with higher identity to fungal (um02581) and the other to plant (um01205) H+-ATPases. Proton pumping activity was 5-fold higher when cells were grown in minimal medium with ethanol compared to cells cultured in rich YPD medium, but total vanadate-sensitive ATPase activity was the same in both conditions. In contrast, the activity in cells cultured in minimal medium with glucose was 2-fold higher than in YPD or ethanol, implicating mechanisms for the regulation of the plasma membrane ATPase activity in U. maydis. Analysis of gene expression of the H+-ATPases from cells grown under different conditions, showed that the transcript expression of um01205 (plant-type) was higher than that of um02581 (fungal-type). The translation of the two proteins was confirmed by mass spectrometry analysis. Unlike baker's yeast and plant H+-ATPases, where the activity is increased by a short incubation with glucose or sucrose, respectively, U. maydis H+-ATPase activity did not change in response to these sugars. Sequence analysis of the two U. maydis H+-ATPases revealed the lack of canonical threonine and serine residues which are targets of protein kinases in Saccharomyces cerevisiae and Arabidopsis thaliana plasma membrane H +-ATPases, suggesting that phosphorylation of the U. maydis enzymes occurs at different amino acid residues.
AB - The fungal and plant plasma membrane H+-ATPases play critical roles in the physiology of yeast, plant and protozoa cells. We identified two genes encoding two plasma membrane H+-ATPases in the basidiomycete Ustilago maydis, one protein with higher identity to fungal (um02581) and the other to plant (um01205) H+-ATPases. Proton pumping activity was 5-fold higher when cells were grown in minimal medium with ethanol compared to cells cultured in rich YPD medium, but total vanadate-sensitive ATPase activity was the same in both conditions. In contrast, the activity in cells cultured in minimal medium with glucose was 2-fold higher than in YPD or ethanol, implicating mechanisms for the regulation of the plasma membrane ATPase activity in U. maydis. Analysis of gene expression of the H+-ATPases from cells grown under different conditions, showed that the transcript expression of um01205 (plant-type) was higher than that of um02581 (fungal-type). The translation of the two proteins was confirmed by mass spectrometry analysis. Unlike baker's yeast and plant H+-ATPases, where the activity is increased by a short incubation with glucose or sucrose, respectively, U. maydis H+-ATPase activity did not change in response to these sugars. Sequence analysis of the two U. maydis H+-ATPases revealed the lack of canonical threonine and serine residues which are targets of protein kinases in Saccharomyces cerevisiae and Arabidopsis thaliana plasma membrane H +-ATPases, suggesting that phosphorylation of the U. maydis enzymes occurs at different amino acid residues.
KW - Basidiomycete
KW - Fungal ATPase
KW - Plants and fungal PMA
KW - Plasma membrane mass spectrometry
KW - Proton pump regulation
KW - Ustilago maydis
UR - http://www.scopus.com/inward/record.url?scp=84885589489&partnerID=8YFLogxK
U2 - 10.1007/s10863-013-9520-1
DO - 10.1007/s10863-013-9520-1
M3 - Artículo
SN - 0145-479X
VL - 45
SP - 477
EP - 490
JO - Journal of Bioenergetics and Biomembranes
JF - Journal of Bioenergetics and Biomembranes
IS - 5
ER -