Unknown

Dataset Information

0

Tetrameric c-di-GMP mediates effective transcription factor dimerization to control Streptomyces development.


ABSTRACT: 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.

SUBMITTER: Tschowri N 

PROVIDER: S-EPMC4151990 | biostudies-literature |

REPOSITORIES: biostudies-literature

Similar Datasets

| S-EPMC5909442 | biostudies-literature
| S-EPMC7005675 | biostudies-literature
| S-EPMC4000578 | biostudies-literature
| S-EPMC4907108 | biostudies-literature
| S-EPMC5499655 | biostudies-literature
| S-EPMC2612001 | biostudies-literature
| S-EPMC11222152 | biostudies-literature
| S-EPMC4140405 | biostudies-literature
| S-EPMC3753962 | biostudies-literature
| S-EPMC6914384 | biostudies-literature