Effects of Bni5 Binding on Septin Filament Organization

Autor: Sarah M. Sterling, Elizabeth A. Booth, Dustin Dovala, Eva Nogales, Jeremy Thorner
Rok vydání: 2016
Předmět:
Models
Molecular
0301 basic medicine
Biochemistry & Molecular Biology
Saccharomyces cerevisiae Proteins
Cell division
1.1 Normal biological development and functioning
Protein subunit
Chemical
yeast (Saccharomyces cerevisiae)
Saccharomyces cerevisiae
macromolecular substances
yeast
Biology
FRET analysis
Septin
Models
Biological
Electron
Microbiology
Article
Turn (biochemistry)
Protein filament
Medicinal and Biomolecular Chemistry
03 medical and health sciences
Models
Structural Biology
Protein Interaction Mapping
Fluorescence Resonance Energy Transfer
Molecular Biology
Microscopy
electron microscopy
Molecular
Biological
Budding yeast
Cell biology
Microscopy
Electron
030104 developmental biology
Förster resonance energy transfer
Models
Chemical
Biochemistry and Cell Biology
Protein Multimerization
analytical ultracentrifugation
Septins
field-flow fractionation
Cytokinesis
Protein Binding
Zdroj: Journal of molecular biology, vol 428, iss 24 Pt B
Booth, EA; Sterling, SM; Dovala, D; Nogales, E; & Thorner, J. (2016). Effects of Bni5 Binding on Septin Filament Organization. Journal of Molecular Biology, 428(24), 4962-4980. doi: 10.1016/j.jmb.2016.10.024. UC Berkeley: Retrieved from: http://www.escholarship.org/uc/item/80x3w0tz
ISSN: 0022-2836
DOI: 10.1016/j.jmb.2016.10.024
Popis: © 2016 The Authors Septins are a protein family found in all eukaryotes (except higher plants) that have roles in membrane remodeling and formation of diffusion barriers and as a scaffold to recruit other proteins. In budding yeast, proper execution of cytokinesis and cell division requires the formation of a collar of circumferential filaments at the bud neck. These filaments are assembled from apolar septin hetero-octamers. Currently, little is known about the mechanisms that control the arrangement and dynamics of septin structures. In this study, we utilized both Förster resonance energy transfer and electron microscopy to analyze the biophysical properties of the septin-binding protein Bni5 and how its association with septin filaments affects their organization. We found that the interaction of Bni5 with the terminal subunit (Cdc11) at the junctions between adjacent hetero-octamers in paired filaments is highly cooperative. Both the C-terminal end of Bni5 and the C-terminal extension of Cdc11 make important contributions to their interaction. Moreover, this binding may stabilize the dimerization of Bni5, which, in turn, forms cross-filament braces that significantly narrow, and impose much more uniform spacing on, the gap between paired filaments.
Databáze: OpenAIRE
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