Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.
The cyclic dinucleotide c-di-GMP is a signaling molecule with diverse functions in cellular physiology. Here, we report that c-di-GMP can assemble into a tetramer that mediates the effective dimerization of a transcription factor, BldD, which controls the progression of multicellular differentiation in sporulating actinomycete bacteria. BldD represses expression of sporulation genes during vegetative growth in a manner that depends on c-di-GMP-mediated dimerization. Structural and biochemical analyses show that tetrameric c-di-GMP links two subunits of BldD through their C-terminal domains, which are otherwise separated by ~10 Å and thus cannot effect dimerization directly. Binding of the c-di-GMP tetramer by BldD is selective and requires a bipartite RXD-X8-RXXD signature. The findings indicate a unique mechanism of protein dimerization and the ability of nucleotide signaling molecules to assume alternative oligomeric states to effect different functions.
Duke Scholars
Altmetric Attention Stats
Dimensions Citation Stats
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Transcription Factors
- Streptomyces
- Spores, Bacterial
- Sequence Alignment
- Molecular Sequence Data
- Models, Molecular
- Dimerization
- Developmental Biology
- Cyclic GMP
- Crystallography, X-Ray
Citation
Published In
DOI
EISSN
Publication Date
Volume
Issue
Start / End Page
Location
Related Subject Headings
- Transcription Factors
- Streptomyces
- Spores, Bacterial
- Sequence Alignment
- Molecular Sequence Data
- Models, Molecular
- Dimerization
- Developmental Biology
- Cyclic GMP
- Crystallography, X-Ray