When a wild-type strain of Escherichia coli contains lactose permease, the accumulation of cyclic AMP (cAMP) by intact cells is inhibited by lactose. This inhibitory effect of lactose is observed in a strain with a mutant cAMP phosphodiesterase and therefore involves a regulation of adenylate cyctase activity. Some E. coli strains carrying mutations in lactose permease show an effect opposite to that of the wild-type strain; the accumulation of cAMP by intact cells is stimulated by lactose, but only when the mutant permease is present. Insertion of lactose permease into the membrane of ceils can produce a change in the specific activity of adenylate cycIase; induction of the wild-type transporter is correlated with a decrease in the specific activity, while implantation of a mutant form of lactose permease can lead to an increase in the specific activity. From these data, it is suggested that the state of the lactose transporter in the cell membrane influences the activity of adenytate cyclase.
Skip Nav Destination
Article navigation
Research Article|
January 01 1981
Stimulation of Escherichia coli adenylate cyclase by lactose in strains carrying mutations in lactose permease
Alan Peterkofsky;
Alan Peterkofsky
1Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20205, U.S.A.
Search for other works by this author on:
Celia Gazdar
Celia Gazdar
1Laboratory of Biochemical Genetics, National Heart, Lung and Blood Institute, National Institutes of Health, Bethesda, Maryland 20205, U.S.A.
Search for other works by this author on:
Publisher: Portland Press Ltd
Received:
November 05 1980
Online ISSN: 1573-4935
Print ISSN: 0144-8463
© 1981 The Biochemical Society
1981
Biosci Rep (1981) 1 (1): 53–60.
Article history
Received:
November 05 1980
Citation
Alan Peterkofsky, Celia Gazdar; Stimulation of Escherichia coli adenylate cyclase by lactose in strains carrying mutations in lactose permease. Biosci Rep 1 January 1981; 1 (1): 53–60. doi: https://doi.org/10.1007/BF01115149
Download citation file:
Sign in
Don't already have an account? Register
Sign in to your personal account
You could not be signed in. Please check your email address / username and password and try again.
Could not validate captcha. Please try again.
Biochemical Society Member Sign in
Sign InSign in via your Institution
Sign in via your InstitutionGet Access To This Article
Cited By
Open Access for all
We offer compliant routes for all authors from 2025. With library support, there will be no author nor reader charges in 5 journals. Check here |
![]() |