title: Cold adaptation in the marine bacterium, Sphingopyxis alaskensis, assessed using quantitative proteomics.
abstract: The cold marine environment constitutes a large proportion of the Earth's biosphere. Sphingopyxis alaskensis was isolated as a numerically abundant bacterium from several cold marine locations, and has been extensively studied as a model marine bacterium. Recently, a metabolic labelling platform was developed to comprehensively identify and quantify proteins from S. alaskensis. The approach incorporated data normalization and statistical validation for the purpose of generating highly confident quantitative proteomics data. Using this approach, we determined quantitative differences between cells grown at 10°C (low temperature) and 30°C (high temperature). Cold adaptation was linked to specific aspects of gene expression: a dedicated protein-folding system using GroESL, DnaK, DnaJ, GrpE, SecB, ClpB and PPIase; polyhydroxyalkanoate-associated storage materials; a link between enzymes in fatty acid metabolism and energy generation; de novo synthesis of polyunsaturated fatty acids in the membrane and cell wall; inorganic phosphate ion transport by a phosphate import PstB homologue; TonB-dependent receptor and bacterioferritin in iron homeostasis; histidine, tryptophan and proline amino acid metabolism; and a large number of proteins without annotated functions. This study provides a new level of understanding on how important marine bacteria can adapt to compete effectively in cold marine environments. This study is also a benchmark for comparative proteomic analyses with other important marine bacteria and other cold-adapted organisms.
authors.affiliation: School of Biotechnology and Biomolecular Sciences, The University of New South Wales, Sydney, NSW 2052, Australia.
authors.forename: Lily
authors.initials: L
authors.lastname: Ting
authors.forename: Timothy J
authors.initials: TJ
authors.lastname: Williams
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Cowley
authors.forename: Federico M
authors.initials: FM
authors.lastname: Lauro
authors.forename: Michael
authors.initials: M
authors.lastname: Guilhaus
authors.forename: Mark J
authors.initials: MJ
authors.lastname: Raftery
authors.forename: Ricardo
authors.initials: R
authors.lastname: Cavicchioli
mesh_terms: D000222:Adaptation, Physiological; D000596:Amino Acids / Q000378:metabolism; D001426:Bacterial Proteins / Q000378:metabolism; D002462:Cell Membrane / Q000502:physiology; D002473:Cell Wall / Q000502:physiology; D003080:Cold Temperature; D005227:Fatty Acids / Q000378:metabolism; D015964:Gene Expression Regulation, Bacterial; D006706:Homeostasis; D007501:Iron / Q000378:metabolism; D017510:Protein Folding; D020543:Proteome / Q000378:metabolism*; D012623:Seawater / Q000737:chemistry / Q000382:microbiology; D042301:Sphingomonadaceae / Q000302:isolation & purification / Q000378:metabolism / Q000502:physiology*
chemical_list: D000596:Amino Acids; D001426:Bacterial Proteins; D005227:Fatty Acids; D020543:Proteome; D007501:Iron