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Volume 131, Issue 1

Adenylate Cyclase Activity During Phenotypic Variation of Free

Abstract

During MgSO-induced modulation of , adenylate cyclase activity, histamine-sensitizing activity (HSA) and the major cell-envelope polypeptides with 28000 and 30000 (X polypeptides) were lost synchronously at a rate which could be accounted for by a simple growth-dilution effect. MgSO and other compounds which induced the above phenotypic change caused little inhibition of adenylate cyclase activity. Nicotinic acid was the sole exception and at 4·1 m-caused 60% inhibition of activity. Lysates of modulated cells, mixed with lysates of unmodulated cells, had no effect on either adenylate cyclase activity or HSA. Protein synthesis was a prerequisite for MgSO-induced modulation and also for the reversal of this process. Exogenous cAMP and dibutyryl cAMP (5 m) had no counteracting effect on MgSO or nicotinic acid-induced modulation. The concentration of MgSO required to induce loss of the X polypeptides (10 to 11 m) was not altered by promoting adenylate cyclase activity by including an activator in the growth medium. In one culture containing 10 m-MgSO and activator, partial loss of the X polypeptides occurred and yet the extracellular cAMP concentration was twice that of cultures without activator and where full expression of the X polypeptides occurred. [H]cAMP-binding activity was detected in cell extracts of several strains of , but antiserum against purified catabote repressor protein gave no reaction with cell extracts. Respiration rates with amino acids were similar for modulated and unmodulated variants and an avirulent strain of . These results are discussed in relation to a possible causal role for adenylate cyclase in modulation of .

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© Society for General Microbiology 1985
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1985-01-01
2024-04-20
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Adenylate Cyclase Activity During Phenotypic Variation of Bordetella pertussis
Microbiology 131, 27 (1985); https://doi.org/10.1099/00221287-131-1-27
/content/journal/micro/10.1099/00221287-131-1-27
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