title: Structural analysis of the elongation factor G protein from the low-temperature-adapted bacterium Arthrobacter globiformis SI55.
abstract: The first structural analysis of elongation factor G (EF-G) from a cold-adapted bacterium is presented. EF-G is an essential protein involved in the elongation process during protein synthesis and is therefore thought to play a crucial role in the low-temperature adaptation of cold-adapted microorganisms. To define its importance, the EF-G gene (fus) from the psychrotolerant bacterium Arthrobacter globiformis SI55 was cloned and sequenced. The deduced primary structure of the elongation factor is composed of 700 amino acids with a predicted molecular mass of 77.4 kDa. A three-dimensional model of the protein was constructed based on the known crystal structures of structurally homologous proteins. Structural features that might potentially be important for activity and flexibility at low temperature were deduced by comparisons with models of the EF-G proteins from the closely related mesophiles Micrococcus luteus and Mycobacterium tuberculosis. These features include a loss in the number of salt bridges in intradomain and interdomain positions, increased solvent interactions mediated by greater charge and polarity on domain surfaces, loop insertions, loss of proline residues in loop structures, and an increase of hydrophobicity in core regions. Specific changes have also been identified in the catalytic domain (G domain) and sites of potential ribosome interaction, which may directly affect guanosine triphosphate (GTP) hydrolysis and elongation rates at low temperature.
authors.affiliation: Ecologie Microbienne, UMR CNRS 5557, Université Lyon I, Villeurbanne, France.
authors.forename: V
authors.initials: V
authors.lastname: Berchet
authors.forename: T
authors.initials: T
authors.lastname: Thomas
authors.forename: R
authors.initials: R
authors.lastname: Cavicchioli
authors.forename: N J
authors.initials: NJ
authors.lastname: Russell
authors.forename: A M
authors.initials: AM
authors.lastname: Gounot
mesh_terms: D000595:Amino Acid Sequence / Q000235:genetics*; D001173:Arthrobacter / Q000235:genetics*; D001426:Bacterial Proteins / Q000737:chemistry / Q000235:genetics*; D003081:Cold Climate; D016982:Micrococcus luteus / Q000235:genetics; D008958:Models, Molecular; D008969:Molecular Sequence Data; D009169:Mycobacterium tuberculosis / Q000235:genetics; D020653:Peptide Elongation Factor G / Q000737:chemistry / Q000235:genetics*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid; D013329:Structure-Activity Relationship
chemical_list: D001426:Bacterial Proteins; D020653:Peptide Elongation Factor G