Abstract
Septins constitute a family of conserved guanine nucleotide binding proteins found in a wide range of organisms from fungi to mammals. Members of the family share a canonical G-domain with N- and C-terminal extensions. G-domains assemble into hetero-oligomeric complexes which form non-polarised filaments or rings. Linear filaments are formed between the G-domains using either the guanine nucleotide binding site (G interface) or N- and C-terminal extensions (NC interface). Sept7 is a unique among the 13 human septins in that it occupies the ends of hexameric building blocks which assemble into non-polarised filaments. To gain insight into its particular properties we performed structural and biochemical studies on Sept7. We solved the crystal structure of a Sept7 dimer in the GDP-bound state. The structure and biochemistry of Sept7 provide new insights into the dynamics of the G interface and outline the differences in the properties of Sept7 compared to the members of group 2 septins.
©2011 by Walter de Gruyter Berlin Boston
Articles in the same Issue
- Editorial
- Highlight on septins
- HIGHLIGHT: EMBO WORKSHOP ‘SEPTINS’
- New insights into the phylogenetic distribution and evolutionary origins of the septins
- Dynamics of septin ring and collar formation in Saccharomyces cerevisiae
- Genetic interactions with mutations affecting septin assembly reveal ESCRT functions in budding yeast cytokinesis
- MLL-SEPTIN gene fusions in hematological malignancies
- Septin roles in tumorigenesis
- Characterization of presynaptic septin complexes in mammalian hippocampal neurons
- Characterization of human septin interactions
- Septin genomics: a road less travelled
- Septin9 is involved in septin filament formation and cellular stability
- Lethal phenotype of mice carrying a Sept11 null mutation
- ARTS, the unusual septin: structural and functional aspects
- Structural and biochemical properties of Sept7, a unique septin required for filament formation
- Septins at the annulus of mammalian sperm
- The mother-bud neck as a signaling platform for the coordination between spindle position and cytokinesis in budding yeast
- Evidence that a septin diffusion barrier is dispensable for cytokinesis in budding yeast
- Septins as key regulators of actin based processes in bacterial infection
Articles in the same Issue
- Editorial
- Highlight on septins
- HIGHLIGHT: EMBO WORKSHOP ‘SEPTINS’
- New insights into the phylogenetic distribution and evolutionary origins of the septins
- Dynamics of septin ring and collar formation in Saccharomyces cerevisiae
- Genetic interactions with mutations affecting septin assembly reveal ESCRT functions in budding yeast cytokinesis
- MLL-SEPTIN gene fusions in hematological malignancies
- Septin roles in tumorigenesis
- Characterization of presynaptic septin complexes in mammalian hippocampal neurons
- Characterization of human septin interactions
- Septin genomics: a road less travelled
- Septin9 is involved in septin filament formation and cellular stability
- Lethal phenotype of mice carrying a Sept11 null mutation
- ARTS, the unusual septin: structural and functional aspects
- Structural and biochemical properties of Sept7, a unique septin required for filament formation
- Septins at the annulus of mammalian sperm
- The mother-bud neck as a signaling platform for the coordination between spindle position and cytokinesis in budding yeast
- Evidence that a septin diffusion barrier is dispensable for cytokinesis in budding yeast
- Septins as key regulators of actin based processes in bacterial infection