Stress-mediated alteration in V-ATPase and V-PPase of Butea monosperma.
The activity and subunit amounts of V-ATPase and V-PPase in various plants of Butea monosperma Taub. (Fabaceae) (ver. Dhak; Palas) growing as a natural inhabitant in varying stress conditions in southeast Rajasthan were studied. Western blot analysis followed by immunological quantification of V-ATPase subunits using specific polyclonal antibodies showed that the subunits A, B, D, E, and c are clearly detectable in all plants, with A, B, and c appearing as intense bands. The other subunits of V-ATPase, viz., C, a, and d, were also detected in majority of the plants. Various subunits exhibited variations in their protein amount in different plants. Besides, a few other clear bands were also detected. Of these, the 30- and 29-kD bands may possibly be Di and Ei. Furthermore, a clear band of V-PPase corresponding to 67-70 kD was also detected. A comparison of the V-ATPase and V-PPase activity revealed that Butea plants in the upper region of the study site showed 70% and 39% higher activity, respectively. Furthermore, the immunological quantification showed that the V-ATPase and V-PPase protein amounts are also higher in the upper Butea plants which have drought stress and, moreover, are also exposed to stronger light intensities for relatively longer duration.
Kumari
Nilima
N
Department of Bioscience and Biotechnology, Banasthali University, P.O. Banasthali Vidyapith, 304 022, Rajasthan, India.
Sharma
Vinay
V
D031290:Butea / Q000201:enzymology*; D008861:Microsomes / Q000201:enzymology; D010940:Plant Proteins / Q000378:metabolism*; D011755:Pyrophosphatases / Q000378:metabolism*; D013312:Stress, Physiological; D025262:Vacuolar Proton-Translocating ATPases / Q000378:metabolism*
D010940:Plant Proteins; D011755:Pyrophosphatases; D025262:Vacuolar Proton-Translocating ATPases