TY - JOUR A1 - Shiyan, Anna A1 - Thompson, Melanie A1 - Köcher, Saskia A1 - Tausendschön, Michaela A1 - Santos, Helena A1 - Hänelt, Inga A1 - Müller, Volker T1 - Glutamine synthetase 2 is not essential for biosynthesis of compatible solutes in Halobacillus halophilus T2 - Frontiers in microbiology N2 - Halobacillus halophilus, a moderately halophilic bacterium isolated from salt marshes, produces various compatible solutes to cope with osmotic stress. Glutamate and glutamine are dominant compatible solutes at mild salinities. Glutamine synthetase activity in cell suspensions of Halobacillus halophilus wild type was shown to be salt dependent and chloride modulated. A possible candidate to catalyze glutamine synthesis is glutamine synthetase A2, whose transcription is stimulated by chloride. To address the role of GlnA2 in the biosynthesis of the osmolytes glutamate and glutamine, a deletion mutant (ΔglnA2) was generated and characterized in detail. We compared the pool of compatible solutes and performed transcriptional analyses of the principal genes controlling the solute production in the wild type strain and the deletion mutant. These measurements did not confirm the hypothesized role of GlnA2 in the osmolyte production. Most likely the presence of another, yet to be identified enzyme has the main contribution in the measured activity in crude extracts and probably determines the total chloride-modulated profile. The role of GlnA2 remains to be elucidated. KW - Halobacillus halophilus KW - glutamine synthetase KW - compatible solutes KW - osmoregulation KW - halophile Y1 - 2014 UR - http://publikationen.ub.uni-frankfurt.de/frontdoor/index/index/docId/52565 UR - https://nbn-resolving.org/urn:nbn:de:hebis:30:3-525650 SN - 1664-302X N1 - Copyright © 2014 Shiyan, Thompson, Köcher, Tausendschön, Santos, Hänelt and Müller. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. VL - 5 IS - Art. 168 SP - 1 EP - 11 PB - Frontiers Media CY - Lausanne ER -