Growth phase-dependent expression and degradation of histones in the thermophilic archaeon Thermococcus zilligii

Dinger, ME, Baillie, GJ and Musgrave, DR (2000) Growth phase-dependent expression and degradation of histones in the thermophilic archaeon Thermococcus zilligii. Molecular Microbiology, 36 4: 876-885. doi:10.1046/j.1365-2958.2000.01904.x


Author Dinger, ME
Baillie, GJ
Musgrave, DR
Title Growth phase-dependent expression and degradation of histones in the thermophilic archaeon Thermococcus zilligii
Journal name Molecular Microbiology   Check publisher's open access policy
ISSN 0950-382X
Publication date 2000-05-01
Year available 2000
Sub-type Article (original research)
DOI 10.1046/j.1365-2958.2000.01904.x
Open Access Status DOI
Volume 36
Issue 4
Start page 876
End page 885
Total pages 10
Publisher BLACKWELL SCIENCE LTD
Language eng
Abstract The majority of cells in nature probably exist in a stationary-phase-like state, due to nutrient limitation in most environments. Studies on bacteria and yeast reveal morphological and physiological changes throughout the stationary phase, which lead to an increased ability to survive prolonged nutrient limitation. However, there is little information on archaeal stationary phase responses. We investigated protein- and lipid-level changes in Thermococcus kodakarensis with extended time in the stationary phase. Adaptations to time in stationary phase included increased proportion of membrane lipids with a tetraether backbone, synthesis of proteins that ensure translational fidelity, specific regulation of ABC transporters (upregulation of some, downregulation of others), and upregulation of proteins involved in coenzyme production. Given that the biological mechanism of tetraether synthesis is unknown, we also considered whether any of the protein-level changes in T. kodakarensis might shed light on the production of tetraether lipids across the same period. A putative carbon-nitrogen hydrolase, a TldE (a protease in Escherichia coli) homologue, and a membrane bound hydrogenase complex subunit were candidates for possible involvement in tetraether-related reactions, while upregulation of adenosylcobalamin synthesis proteins might lend support to a possible radical mechanism as a trigger for tetraether synthesis.
Keyword Ionization Mass-Spectrometry
Escherichia-Coli
Dna-Binding
Methanothermus-Fervidus
Stationary-Phase
Gene-Expression
Isolate An1
Protein
Transcription
Topology
Q-Index Code C1
Q-Index Status Provisional Code
Grant ID 247153
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collection: ResearcherID Downloads - Archived
 
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