TY - JOUR
T1 - Purification and characterization of an intracellular aspartyl acid proteinase (pumAi) from Ustilago maydis
AU - Mercado-Flores, Yuridia
AU - Trejo-Aguilar, Adriana
AU - Ramĩrez-Zavala, Bernardo
AU - Villa-Tanaca, Lourdes
AU - Hernández-Rodríguez, César
PY - 2005/2
Y1 - 2005/2
N2 - The intracellular proteinase pumAi in Ustilago maydis has been associated with yeast-mycelium dimorphic transition. The proteinase was purified from a cell-free extract by ammonium sulfate fractionation and chromatographic steps including hydrophobic interactions on a Phenyl Superose column, ion exchange on a Mono Q column, and gel filtration on Superose 12 columns. The enzyme has a mass of 35.3-36.6 kDa, a pH and temperature optimum of 4.0 and 40°C, respectively, and a pi of 5.5. The enzyme degraded hemoglobin, gelatin, albumin, and casein, but not collagen, and the enzymatic activity was strongly inhibited by pepstatin A, an aspartyl proteinase-specific inhibitor. The biochemical characteristics of pumAi are similar to other fungal intracellular aspartyl proteinases, however, this is the first biochemical characterization of a basidiomycete proteinase probably associated with dimorphic yeast-mycelium transition.
AB - The intracellular proteinase pumAi in Ustilago maydis has been associated with yeast-mycelium dimorphic transition. The proteinase was purified from a cell-free extract by ammonium sulfate fractionation and chromatographic steps including hydrophobic interactions on a Phenyl Superose column, ion exchange on a Mono Q column, and gel filtration on Superose 12 columns. The enzyme has a mass of 35.3-36.6 kDa, a pH and temperature optimum of 4.0 and 40°C, respectively, and a pi of 5.5. The enzyme degraded hemoglobin, gelatin, albumin, and casein, but not collagen, and the enzymatic activity was strongly inhibited by pepstatin A, an aspartyl proteinase-specific inhibitor. The biochemical characteristics of pumAi are similar to other fungal intracellular aspartyl proteinases, however, this is the first biochemical characterization of a basidiomycete proteinase probably associated with dimorphic yeast-mycelium transition.
KW - Aspartyl proteinase
KW - Ustilago maydis
KW - Yeast-mycelium transition
UR - http://www.scopus.com/inward/record.url?scp=20444493186&partnerID=8YFLogxK
U2 - 10.1139/w04-125
DO - 10.1139/w04-125
M3 - Artículo
C2 - 16091776
SN - 0008-4166
VL - 51
SP - 171
EP - 175
JO - Canadian Journal of Microbiology
JF - Canadian Journal of Microbiology
IS - 2
ER -