Journal of Bacteriology, February 2005, p. 923-929, Vol. 187, No. 3
0021-9193/05/$08.00+0 doi:10.1128/JB.187.3.923-929.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
Growth Kinetics of Extremely Halophilic Archaea (Family Halobacteriaceae) as Revealed by Arrhenius Plots
Jessie L. Robinson,1
Brandy Pyzyna,1
Rachelle G. Atrasz,1
Christine A. Henderson,1
Kira L. Morrill,1
Anna Mae Burd,1
Erik DeSoucy,1
Rex E. Fogleman III,1
John B. Naylor,1
Sarah M. Steele,1
Dawn R. Elliott,1
Kathryn J. Leyva,2 and
Richard F. Shand1*
Department of Biological Sciences, Northern Arizona University, Flagstaff,1
Department of Microbiology, Arizona College of Osteopathic Medicine, Midwestern University, Glendale, Arizona2
Received 22 August 2004/
Accepted 31 October 2004
Members of the family Halobacteriaceae in the domain Archaea are obligate extreme halophiles. They occupy a variety of hypersaline environments, and their cellular biochemistry functions in a nearly saturated salty milieu. Despite extensive study, a detailed analysis of their growth kinetics is missing. To remedy this, Arrhenius plots for 14 type species of the family were generated. These organisms had maximum growth temperatures ranging from 49 to 58°C. Nine of the organisms exhibited a single temperature optimum, while five grew optimally at more than one temperature. Generation times at these optimal temperatures ranged from 1.5 h (Haloterrigena turkmenica) to 3.0 h (Haloarcula vallismortis and Halorubrum saccharovorum). All shared an inflection point at 31 ± 4°C, and the temperature characteristics for 12 of the 14 type species were nearly parallel. The other two species (Natronomonas pharaonis and Natronorubrum bangense) had significantly different temperature characteristics, suggesting that the physiology of these strains is different. In addition, these data show that the type species for the family Halobacteriaceae share similar growth kinetics and are capable of much faster growth at higher temperatures than those previously reported.
* Corresponding author. Mailing address: Department of Biological Sciences, Northern Arizona University, Flagstaff, AZ 86011-5640. Phone: (928) 523-9970. Fax: (928) 523-7500. E-mail: Richard.Shand{at}nau.edu.
Journal of Bacteriology, February 2005, p. 923-929, Vol. 187, No. 3
0021-9193/05/$08.00+0 doi:10.1128/JB.187.3.923-929.2005
Copyright © 2005, American Society for Microbiology. All Rights Reserved.
This article has been cited by other articles:
-
Bidle, K. A., Kirkland, P. A., Nannen, J. L., Maupin-Furlow, J. A.
(2008). Proteomic analysis of Haloferax volcanii reveals salinity-mediated regulation of the stress response protein PspA. Microbiology
154: 1436-1443
[Abstract]
[Full Text]
-
Allen, M. A., Goh, F., Leuko, S., Echigo, A., Mizuki, T., Usami, R., Kamekura, M., Neilan, B. A., Burns, B. P.
(2008). Haloferax elongans sp. nov. and Haloferax mucosum sp. nov., isolated from microbial mats from Hamelin Pool, Shark Bay, Australia. Int. J. Syst. Evol. Microbiol.
58: 798-802
[Abstract]
[Full Text]
-
Fukushima, E., Shinka, Y., Fukui, T., Atomi, H., Imanaka, T.
(2007). Methionine Sulfoxide Reductase from the Hyperthermophilic Archaeon Thermococcus kodakaraensis, an Enzyme Designed To Function at Suboptimal Growth Temperatures. J. Bacteriol.
189: 7134-7144
[Abstract]
[Full Text]
Copyright © 2005 by the American Society for Microbiology. All rights reserved.