bioRxiv Science⌕ Search

Biology subjects

Devlin, L.

Publications and source records attributed to Devlin, L..

2 recordsLinked to original sources

Acetate promotes nutritional adaptation in Escherichia coli

The long-held view that acetate, one of the main fermentation by-products of Escherichia coli, is toxic to microbial growth is currently challenged. Here, we demonstrate that acetate promotes E. coli adaptation to nutrient changes by accelerating growth resumption, with as little as 250 {micro}M acetate being sufficient to shorten the lag phase by several hours. Acetate was found to be consumed via acetyl-CoA synthetase very early after the nutrient change. Transcriptomics, metabolomics and 13C-isotope labeling experiments show that acetate replenishes metabolic pools in the tricarboxylic acid cycle and upper glycolysis. Single-cell analyses reveal that acetate increases the adaptation speed of individual cells switching to the new nutrient. We conclude that the reuse of excreted acetate by E. coli facilitates metabolic adaptation by transiently replenishing central metabolite pools. This work identifies an unexpected role of acetate in the nutritional adaptation of E. coli, providing new insights into the physiological relevance of overflow metabolism. HighlightsO_LIAcetate facilitates E. coli adaptation from one nutrient to another. C_LIO_LILess than 250 {micro}M acetate is sufficient to halve lag times. C_LIO_LIAcetate helps replenish metabolite pools in central carbon metabolism. C_LIO_LIAcetate excretion is an adaptative strategy to overcome resource fluctuations. C_LI

systems biology↗

Proteomic profiling of the oncogenic septin 9 reveals isoform-specific interactions in breast cancer cells

Septins are a family of multimeric GTP-binding proteins, which are abnormally expressed in cancer. Septin 9 (SEPT9) is an essential and ubiquitously expressed septin with multiple isoforms, which have differential expression patterns and effects in breast cancer cells. It is unknown, however, if SEPT9 isoforms associate with different molecular networks and functions. Here, we performed a proteomic screen in MCF-7 breast cancer cells to identify the interactome of GFP-SEPT9 isoforms 1, 4 and 5, which vary significantly in their N-terminal extensions. While all three isoforms associated with SEPT2 and SEPT7, the truncated SEPT9_i4 and SEPT9_i5 interacted with septins of the SEPT6 group more promiscuously than SEPT9_i1, which bound predominately SEPT8. Spatial mapping and functional clustering of non-septin partners showed isoform-specific differences in interactions with proteins of distinct subcellular organelles (e.g., nuclei, centrosomes, cilia) and functions such as cell signaling and ubiquitination. Notably, the interactome of the full length SEPT9_i1 was more enriched in cytoskeletal regulators, while the truncated SEPT9_i4 and SEPT9_i5 exhibited preferential and isoform-specific interactions with nuclear, signaling and ubiquitinating proteins. These data provide evidence for isoform-specific interactions, which arise from truncations in the N-terminal extensions of SEPT9, and point to novel roles in the pathogenesis of breast cancer.

cell biology↗