Biological invasion by alien invasive species is now recognized as one of the major threats to native species and ecosystems. Parthenium weed ( Parthenium hysterophorus L.), an alien invasive weed species, is spreading throughout Pakistan. Worldwide, it has been designated as one of the most troublesome weed species. The adverse effects of this weed on human beings, livestock, crop production, and biodiversity are well-documented. As a result of a lack of information on its spread in Pakistan since its invasion, a phytosociological survey, with special reference to parthenium weed, was carried out in Islamabad from August-October 2002. Six main sectors of Islamabad were selected for sampling. The phytosociological survey of these sectors of Islamabad revealed a total of 30 weed species to be associated with P. hysterophorus . The survey also showed a high relative frequency, relative density, and importance value of P. hysterophorus in general; however, the percentage relative frequency of the weed in these sectors ranged from 10.6-30.3%. This survey revealed that P. hysterophorus had an appreciable degree of sociability with Senna occidentalis (L.) Link, Malvastrum coromandelianum (L.) Garcke and Lantana camara (L.) . The data on the association of L. camara with P. hysterophorus suggests that a transition phase of competition or succession is in progress between these two alien species. The population of many common medicinal plants growing in the wastelands of Islamabad might be rapidly declining because of the aggressive colonization by P. hysterophorus . The ever-increasing infestation of this weed in urban areas also poses a serious threat to the health of the inhabitants of Islamabad.
Calcium-dependent association with a detergent-extracted particulate fraction was used as the first step in the purification of a group of phospholipid binding proteins. Elution of the detergent-insoluble fraction with excess ethylene glycol bis(beta-aminoethyl ether)-N,N,N',N'-tetraacetic acid (EGTA) resulted in the release of several soluble proteins, termed calcium-activated proteins or CAPs. In the present paper, we describe the simultaneous purification of these CAPs and characterize their interaction with phospholipid, actin, and calmodulin. Partial sequence analysis has identified the majority of the CAPs as members of the annexin family of calcium and phospholipid binding proteins. Two additional CAPs may be novel proteins, one of which appears to be an annexin protein. All CAPs demonstrated Ca2(+)-dependent binding to phosphatidylserine vesicles but did not bind to phosphatidylcholine vesicles. The majority of CAPs exhibited Ca2(+)-dependent binding to F-actin; however, only CAP-III affected the rate of conversion of G-actin to F-actin. The interaction of CAP-III and lipocortin-85 with F-actin resulted in a Ca2(+)-dependent increase in both light scattering and sedimentation of F-actin under comparatively low centrifugal force. In contrast, only lipocortin-85 caused the formation of F-actin bundles. Although all of the CAPs bound to a calmodulin affinity column in a Ca2(+)-dependent manner, attempts to demonstrate binding of CAPs to native calmodulin were unsuccessful. These studies therefore document the similar behavior of the CAPs toward phospholipid and calmodulin but clearly show that F-actin binding or bundling is not a general property of these proteins. The reported purification procedure should allow further comparative studies of these proteins.
SUMMARYThe ability of the ericoid mycorrhizal endophyte to utilize a range of proteins as substrates for growth is assessed in liquid culture and in mycorrhizal association with host plants. Some aspects of proteolytic enzyme production are also investigated.The fungus readily utilizes the soluble protein bovine serum albumin (BSA) as sole nitrogen and carbon source, and produces lower yields on less soluble plant and animal proteins. Maximum yields of endophyte on all substrates were obtained in the pH range 3 to 5. Infection provides a significant enhancement of plant growth on agar over this pH range on most of the proteins. Yields and nitrogen contents of mycorrhizal plants grown on cellulose sheets with BSA as sole N source were significantly higher than those of the uninfected controls, which were unable to use protein.Using a chromogenic substrate it was shown that the pH optimum for enzyme activity is comparable with that for utilization of protein in pure culture and in mycorrhizal association. Non-mycorrhizal plants produced negligible proteolytic activity.The significance of these observations is discussed in relation to the nutrition of both host and fungus in the natural environment, and the broader ecological implications of the results are assessed.
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