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The activity of M.echinospora proteases was investigated over a broad pH range (pH 5 –9.5) in the following buffers:150 mM sodium citrate (pH 3 –4),150 mM sodium acetate/acetic acid (4 –6.5),sodium phosphate (6.5 –7.5),Tris/HCl (pH 7.5 –9).Protease activity was found to have an optimum of pH 7 throughout growth (data not shown).No differences were observed in the pH optima of the proteases from different media,or culture conditions.An indication of proteolytic class was determined by incubation of culture supernatants with a range of protease inhibitors,according to the method of Dunn (1989).Protease inhibitor studies were conducted on samples taken from the stationary phase of YEME grown cultures.The extracellular proteases of M.echinospora were subject to significant inhibition of proteolytic activity with TLCK (Tosyl-lysyl-chloromethyl-ketone; an inhibitor of Trypsinlike serine proteases,100 mM),TPCK (Tosyl-phenylalanyl-chloromethyl-ketone; an inhibitor of chymotrypsin-like serine proteases,100 mM),E-64 (an inhibitor of cysteine proteases,1 mM),and Pepstatin (an inhibitor of aspartic proteases,1 mM).Inhibition of protease activity by EDTA (an inhibitor of metalloproteases,100 mM) was less significant.These data suggest that M.echinospora produces at least three types of proteases during growth (Table 2).
To examine the possible physiological role of the proteolytic enzymes,protease inhibitors were applied onto the surface of growing cultures (on filter papers impregnated with the inhibitor).Sporulation was inhibited by the application of TLCK and TPCK,established by the absence of the culture darkening (Figure 2) and confirmed by microscopic impression mounts of the culture surface (data not shown).This suggests a link between a serine protease and morphological differentiation in M.echinospora.Given that morphological differentiation in M.echinospora was accompanied by the production of extracellular proteolytic enzymes,and that differentiation can be inhibited by the application of protease inhibitors,it is reasonable to assume they play some role in sporulation in this organism.It has been shown that extracellular proteolytic enzymes in bacteria may be synthesised in response to the presence of an inducing substrate within the medium,or when growth conditions are suboptimal for growth.In Bacillus protease production and sporulation have been linked (Ochi 1985) and genes having pleiotropic effects on both processes have been identified (Piggot and Coote 1976).
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The activity of M.echinospora proteases was investigated over a broad pH range (pH 5 –9.5) in the following buffers:150 mM sodium citrate (pH 3 –4),150 mM sodium acetate/acetic acid (4 –6.5),sodium phosphate (6.5 –7.5),Tris/HCl (pH 7.5 –9).Protease activity was found to have an optimum of pH 7 throughout growth (data not shown).No differences were observed in the pH optima of the proteases from different media,or culture conditions.An indication of proteolytic class was determined by incubation of culture supernatants with a range of protease inhibitors,according to the method of Dunn (1989).Protease inhibitor studies were conducted on samples taken from the stationary phase of YEME grown cultures.The extracellular proteases of M.echinospora were subject to significant inhibition of proteolytic activity with TLCK (Tosyl-lysyl-chloromethyl-ketone; an inhibitor of Trypsinlike serine proteases,100 mM),TPCK (Tosyl-phenylalanyl-chloromethyl-ketone; an inhibitor of chymotrypsin-like serine proteases,100 mM),E-64 (an inhibitor of cysteine proteases,1 mM),and Pepstatin (an inhibitor of aspartic proteases,1 mM).Inhibition of protease activity by EDTA (an inhibitor of metalloproteases,100 mM) was less significant.These data suggest that M.echinospora produces at least three types of proteases during growth (Table 2).
To examine the possible physiological role of the proteolytic enzymes,protease inhibitors were applied onto the surface of growing cultures (on filter papers impregnated with the inhibitor).Sporulation was inhibited by the application of TLCK and TPCK,established by the absence of the culture darkening (Figure 2) and confirmed by microscopic impression mounts of the culture surface (data not shown).This suggests a link between a serine protease and morphological differentiation in M.echinospora.Given that morphological differentiation in M.echinospora was accompanied by the production of extracellular proteolytic enzymes,and that differentiation can be inhibited by the application of protease inhibitors,it is reasonable to assume they play some role in sporulation in this organism.It has been shown that extracellular proteolytic enzymes in bacteria may be synthesised in response to the presence of an inducing substrate within the medium,or when growth conditions are suboptimal for growth.In Bacillus protease production and sporulation have been linked (Ochi 1985) and genes having pleiotropic effects on both processes have been identified (Piggot and Coote 1976).
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