Examination of processing of the rat liver mitochondrial F1-ATPase beta subunit precursor protein by high-resolution 2D-gel electrophoresis.
We report the one-step processing of the rat liver beta-F1-ATPase precursor protein, as examined by high resolution 2D-gel electrophoresis. Proteolytic cleavage of the positively charged mitochondrial targeting signal of the precursor promotes decreases in both the molecular weight (approximately 3 kDa) and the isoelectric point (approximate 0.2 pH unit) of the protein. The results obtained illustrate the usefulness of this technique, since it takes advantage of both results of the maturation process, for molecular characterization of the processing of mitochondrial precursor proteins.
Santarén
J F
JF
Departamento de Biología Molecular, Centro de Biología Molecular Severo Ochoa, (CSIC-UAM), Universidad Autónoma de Madrid, Spain.
Alconada
A
A
Cuezva
J M
JM
D000818:Animals; D015180:Electrophoresis, Gel, Two-Dimensional; D007526:Isoelectric Point; D008930:Mitochondria, Liver / Q000201:enzymology*; D008970:Molecular Weight; D011498:Protein Precursors / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D006180:Proton-Translocating ATPases / Q000378:metabolism*; D051381:Rats
D011498:Protein Precursors; D006180:Proton-Translocating ATPases