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Karas, B.

Publications and source records attributed to Karas, B..

2 recordsLinked to original sources

Scaling laws in enzyme function reveal a new kind of biochemical universality

All life on Earth is unified by its use of a shared set of component chemical compounds and reactions, providing a detailed model for universal biochemistry. However, this notion of universality is specific to currently observed biochemistry and does not allow quantitative predictions about examples not yet observed. Here we introduce a more generalizable concept of biochemical universality, more akin to the kind of universality discussed in physics. Using annotated genomic datasets including an ensemble of 11955 metagenomes and 1282 archaea, 11759 bacteria and 200 eukaryotic taxa, we show how four of the major enzyme functions - the oxidoreductases, transferases, hydrolases and ligases - form universality classes with common scaling behavior in their relative abundances observed across the datasets. We verify these universal scaling laws are not explained by the presence of compounds, reactions and enzyme functions shared across all known examples of life. We also demonstrate how a consensus model for the last universal common ancestor (LUCA) is consistent with predictions from these scaling laws, with the exception of ligases and transferases. Our results establish the existence of a new kind of biochemical universality, independent of the details of the component chemistry, with implications for guiding our search for missing biochemical diversity on Earth, or other for any biochemistries that might deviate from the exact chemical make-up of life as we know it, such as at the origins of life, in alien environments, or in the design of synthetic life.

systems biology↗

Intragenic Complementation of Cellulose Synthase-Like D1 alleles in Root Hair Development

Root hair cells form the primary interface of plants with the soil environment, playing key roles in nutrient uptake and plant defense. In addition, they are typically the first cells infected by nitrogen-fixing soil bacteria during the root nodule symbiosis. Here we report a role for the Cellulose Synthase-Like D1 (CSLD1) gene in root hair development in Lotus japonicus. CSLD1 belongs to the cellulose synthase protein family that includes cellulose synthases, and cellulose synthase-like proteins, the latter thought to be involved in the biosynthesis of hemicellulose. We describe 11 csld1 mutant alleles that have either short (Ljcsld1-1) or variable length roots hairs (Ljcsld1-2 to 11). Examination of Ljcsld1-1 and one variable-length root hair mutant, Ljcsld1-6 showed increased root hair cell wall thickness, which in Ljcsld1-1 was more pronounced, suggesting a possible link with the defect in root nodule symbiosis. In addition, Ljcsld1-1 heterozygotes had intermediate root hair lengths, between those of wild type and the homozygotes. Intragenic complementation was observed between alleles with mutations in the N-terminal domain and other alleles, suggesting modularity of CSLD1 function and that it may operate as a homodimer or multimer. One sentence summaryThis research describes novel gain- and loss-of-function mutations at the Lotus japonicus CELLULOSE SYNTHASE-LIKE D1 locus and analyzes their impact on root hair development.

plant biology↗