Open AccessPreferential synthesis of stress proteins in stationary Zymomonas mobilis cells
Author(s) -
Michel G.P.F.,
Starka J.
Publication year - 1987
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.1574-6968.1987.tb02173.x
Subject(s) - zymomonas mobilis , chemistry , biophysics , stress (linguistics) , biochemistry , microbiology and biotechnology , biology , fermentation , ethanol fuel , linguistics , philosophy
Most of the stress proteins induced after exposure of Zymomonas mobilis to sublethal heat or ethanol shock were shown to be major cellular proteins even in unshocked bacteria. However, a new polypeptide (E 18.5) was detected only after thermal or alcoholic stress. The appearance of E 18.5 was shown to be unrelated to a degradation process but to depend on protein synthesis. Induction of E 18.5 synthesis was controlled at the transcription level and the same conclusion can be drawn for other stress proteins. When cells entered the stationary phase, most of the proteins synthesized were of the stress protein group, including E 18.5. It is suggested that stress proteins, particularly E 18.5, could play an important role in the physiology of Z. mobilis and that they could be directly or indirectly involved in the mechanism of ethanol tolerance.