Open AccessIsolation of a cAMP‐requiring mutant in Escherichia coli K‐12: evidence of growth regulation via N ‐acetylglucosamine metabolism controlled by cAMP
Author(s) -
Utsumi Ryutaro,
Noda Manjiro,
Kawamukai Makoto,
Komano Tohru
Publication year - 1988
Publication title -
fems microbiology letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.899
H-Index - 151
eISSN - 1574-6968
pISSN - 0378-1097
DOI - 10.1111/j.1574-6968.1988.tb02941.x
Subject(s) - mutant , n acetylglucosamine , glucosamine , adenylate kinase , biochemistry , biology , amino sugar , cyclase , metabolism , mutation , acetylglucosamine , stringent response , adenosine , gene , enzyme
An adenylate cyclase gene ( cya ) mutant was mutagenized and an adenosine 3,5‐cyclic monophosphate (cAMP)‐requiring mutant (KM8161) was obtained on Davis minimal medium containing glucose in the presence or absence of cAMP. KM8161 also required N ‐acetylglucosamine for its growth instead of cAMP. Furthermore, the mutant could use neither glucosamine nor N ‐acetylglucosamine as the carbon source. These results indicate that the cAMP‐requiring property is due to multiple mutations of a few genes involved in amino sugar metabolism in addition to cya . By genetic analysis of KM8161, one gene, which was tentatively termed cidA and located near 2 min on the chromosomal map, proved to be defective. Reversion of cidA mutation in KM8161 resulted in recovery of not only the cAMP‐requiring phenotype but also non‐utilization of amino sugars. When both cAMP and N ‐acetylglucosamine or glucosamine were added to the culture medium for KM8161, only N ‐acetylglucosamine could be utilized as the carbon source. These studies s strongly suggest that the cidA or cya mutation in KM8161 causes deficiency in different stages of amino sugar metabolism and the regulatory circuit of growth by cAMP is mediated via control of N ‐acetylglucosamine metabolism.