scholarly journals 3',5'-cyclic adenosine monophosphate dependent xylose lethal phenomenon in Escherichia coli.

1976 ◽  
Vol 40 (1) ◽  
pp. 197-201
Author(s):  
Rikizo AONO ◽  
Makari YAMASAKI ◽  
Gakuzo TAMURA
Genetics ◽  
1972 ◽  
Vol 70 (1) ◽  
pp. 175-180
Author(s):  
LaDonna Immken ◽  
David Apirion

ABSTRACT 3″,5″ cyclic-AMP (cAMP) will stimulate the rate of tryptophanase synthesis in Escherichia coli cultures induced with tryptophan. Adding cAMP after the initiation of messenger RNA synthesis was blocked by rifampicin, did not stimulate tryptophanase synthesis. This indicates that cAMP acts at initiation of either transcription or translation and not at the level of chain elongation of either the messenger or the polypeptide chain.


1980 ◽  
Vol 26 (3) ◽  
pp. 393-396 ◽  
Author(s):  
Ann D. E. Fraser ◽  
Hiroshi Yamazaki

The aerobic catabolism of glycerol depends on the expression of the glpK operon specifying a glycerol kinase and the glpD operon specifying an sn-glycerol-3-phosphate (G3P) dehydrogenase. It has not been clearly established how the expression of these operons is dependent on adenosine 3′,5′-cyclic monophosphate (cAMP). We have isolated a promoterlike mutant (CA8306B) which, owing to a mutation in the glpK operon, can utilize glycerol in the absence of cAMP. Glycerol kinase and G3P dehydrogenase are inducible in CA8306B and its wild-type parent CA8000. The induced level of glycerol kinase in CA8306B is 30% that of CA8000and this level is increased fivefold by the addition of cAMP. However, the induced level of G3P dehydrogenase in CA8306B is similar to that of CA8000 and is unaffected by cAMP addition. These results suggest that the promotion of the glpK operon requires cAMP whereas the promotion of the glpD operon does not.


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