Bacterial lipid droplets bind to DNA via an intermediary protein that enhances survival under stress.
basic_science · Level V
Where this comes from
- Record sourced from PubMed, PMID 28681845.
- Also identified by DOI 10.1038/ncomms15979 and PMC identifier 5504291.
- Licence recorded as CC BY.
- The licence permits redistribution, so the abstract is shown in full and the full text is available from the publisher.
Abstract
Lipid droplets (LDs) are multi-functional organelles consisting of a neutral lipid core surrounded by a phospholipid monolayer, and exist in organisms ranging from bacteria to humans. Here we study the functions of LDs in the oleaginous bacterium Rhodococcus jostii. We show that these LDs bind to genomic DNA through the major LD protein, MLDS, which increases survival rate of the bacterial cells under nutritional and genotoxic stress. MLDS expression is regulated by a transcriptional regulator, MLDSR, that binds to the operator and promoter of the operon encoding both proteins. LDs sequester MLDSR, controlling its availability for transcriptional regulation. Our findings support the idea that bacterial LDs can regulate nucleic acid function and facilitate bacterial survival under stress.
Medical subject headings
- Bacterial Proteins
- DNA, Bacterial
- Gene Expression Regulation, Bacterial
- Lipid Droplet Associated Proteins
- Lipid Droplets
- Rhodococcus