TY - JOUR
T1 - Carbon and nitrogen sources have no impact on the organization and composition of ustilago maydis respiratory supercomplexes
AU - Matuz-Mares, Deyamira
AU - Flores-Herrera, Oscar
AU - Guerra-Sánchez, Guadalupe
AU - Romero-Aguilar, Lucero
AU - Vázquez-Meza, Héctor
AU - Matus-Ortega, Genaro
AU - Martínez, Federico
AU - Pardo, Juan Pablo
N1 - Publisher Copyright:
© 2021 by the authors. Li-censee MDPI, Basel, Switzerland.
PY - 2021/1
Y1 - 2021/1
N2 - Respiratory supercomplexes are found in mitochondria of eukaryotic cells and some bacteria. A hypothetical role of these supercomplexes is electron channeling, which in principle should increase the respiratory chain efficiency and ATP synthesis. In addition to the four classic respiratory complexes and the ATP synthase, U. maydis mitochondria contain three type II NADH dehydrogenases (NADH for reduced nicotinamide adenine dinucleotide) and the alternative oxi-dase. Changes in the composition of the respiratory supercomplexes due to energy requirements have been reported in certain organisms. In this study, we addressed the organization of the mi-tochondrial respiratory complexes in U. maydis under diverse energy conditions. Supercomplexes were obtained by solubilization of U. maydis mitochondria with digitonin and separated by blue native polyacrylamide gel electrophoresis (BN-PAGE). The molecular mass of supercomplexes and their probable stoichiometries were 1200 kDa (I1:IV1), 1400 kDa (I1:III2), 1600 kDa (I1:III2:IV1), and 1800 kDa (I1:III2:IV2). Concerning the ATP synthase, approximately half of the protein is present as a dimer and half as a monomer. The distribution of respiratory supercomplexes was the same in all growth conditions. We did not find evidence for the association of complex II and the alternative NADH dehydrogenases with other respiratory complexes.
AB - Respiratory supercomplexes are found in mitochondria of eukaryotic cells and some bacteria. A hypothetical role of these supercomplexes is electron channeling, which in principle should increase the respiratory chain efficiency and ATP synthesis. In addition to the four classic respiratory complexes and the ATP synthase, U. maydis mitochondria contain three type II NADH dehydrogenases (NADH for reduced nicotinamide adenine dinucleotide) and the alternative oxi-dase. Changes in the composition of the respiratory supercomplexes due to energy requirements have been reported in certain organisms. In this study, we addressed the organization of the mi-tochondrial respiratory complexes in U. maydis under diverse energy conditions. Supercomplexes were obtained by solubilization of U. maydis mitochondria with digitonin and separated by blue native polyacrylamide gel electrophoresis (BN-PAGE). The molecular mass of supercomplexes and their probable stoichiometries were 1200 kDa (I1:IV1), 1400 kDa (I1:III2), 1600 kDa (I1:III2:IV1), and 1800 kDa (I1:III2:IV2). Concerning the ATP synthase, approximately half of the protein is present as a dimer and half as a monomer. The distribution of respiratory supercomplexes was the same in all growth conditions. We did not find evidence for the association of complex II and the alternative NADH dehydrogenases with other respiratory complexes.
KW - Mitochondrial supercomplexes
KW - Respiratory complexes
KW - Ustilago maydis mitochondria
UR - http://www.scopus.com/inward/record.url?scp=85099860097&partnerID=8YFLogxK
U2 - 10.3390/jof7010042
DO - 10.3390/jof7010042
M3 - Artículo
C2 - 33440829
AN - SCOPUS:85099860097
SN - 2309-608X
VL - 7
SP - 1
EP - 14
JO - Journal of Fungi
JF - Journal of Fungi
IS - 1
M1 - 42
ER -