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PubMed2026

OscillomeR infers ultradian oscillations and targets of the Hes family.

The Hes family, basic-helix-loop-helix transcription factors and downstream effectors of Notch signaling, regulate the fate choices of pancreatic progenitors, muscle stem cells, neuronal progenitors, and presomitic mesoderm cells. Bioluminescence imaging (BLI) has revealed ultradian oscillatory dynamics of Hes-family members Hes1, Hes5, and Hes7. However, identifying which of the Hes target genes also oscillate remains challenging due to the time-consuming and costly nature of tracking individual target genes using BLI. Here, we propose OscillomeR, a computational framework that reconstructs ultradian oscillations from RNA-sequencing data to identify oscillatory target genes at high throughput. OscillomeR predicts thousands of oscillatory genes in synchronized or unsynchronized cell types, identifying both known and novel Hes-family targets. It also captures the dynamic rewiring of gene-regulatory networks during cell differentiation. Overall, OscillomeR is an effective tool for elucidating the functions of oscillatory transcription factors at the genomic scale.

Hes family↗
PubMed2026

Genetic Diversity and Population Structure of Zambian Indigenous Cattle.

A study was conducted to determine the genetic diversity of Zambian indigenous cattle using microsatellites. In Zambia, cattle provide draft power, food, manure and generate income. DNA extraction followed the Qiagen protocol, and Arlequin V3.0 was used for data analysis. 72 unrelated animals from three regions, Eastern (Angoni), Southern (Tonga) and Western (Barotse), were sampled. 315 alleles observed were higher in TGLA 263 (106 bp) with 0.861, 0.824 and 0.753, BMS650 (160 bp) with 0.710 and SPS 115 (248 bp) with 0.581, 0.710 and 0.794 for Angoni, Tonga and Barotse, respectively. Effective allele frequency was 4.521 ± 0.351, 4.246 ± 0.299 and 3.888 ± 0.289 for Angoni, Tonga and Barotse, respectively. Global deficit of heterozygotes across populations (Fit) amounted to 4.2%. Overall mean deficit of heterozygotes (Fis = 1%), genetic differentiation among breeds (Fst = 3.2%),, and genetic flow between populations (Nm = 11.3) ranged from RM 067 (40.564) to BLI (3.016). Analysis of molecular variance revealed 2.7% genetic variation among populations and 97.3% within the cattle population, with a mean genetic diversity of 0.753. Structure analysis (PCoA) demonstrated the presence of two subpopulations in which all three populations are represented and these two groups showed evidence of substructuring. In the Bayesian analysis, Tonga and Barotse populations were clustered together, while the Angoni were separated from the rest of the populations in K = 2. There was no evidence of panmixia and linkage equilibrium; the VD (9.153) value is greater than L (5.929), indicating that the population was in equilibrium. This study presents a comprehensive genetic characterisation of indigenous cattle in Zambia, which is important for further studies.

Animals↗
PubMed2026

Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions.

In signaling cascades, signaling proteins often encode multiple domains or motifs, which presents the possibility for avidity -- where multivalent binding drastically increases interaction strength and duration. However, predicting and validating multivalent interactions that interact with avidity is a challenge. Here, we integrate mechanistic modeling, structure-based analysis, and experimental approaches as a framework for defining the conditions under which avidity plays a role. We explore the tandem SH2 domain family of interactions with bisphosphorylated partners as a multivalent archetype, which encompasses key secondary messengers in tyrosine kinase signaling networks. Theoretical modeling suggests that maximum avidity occurs with closely spaced tyrosine phosphorylation sites combined with moderate monovalent affinities - exactly around the innate range of SH2 domain affinity - or with phosphorylation sites separated by sufficiently flexible linkers. Surprisingly, despite sequence diversity, structure-based analysis showed relatively conserved three-dimensional spacing between SH2 domains across all tandem SH2 families, which we corroborate experimentally, suggesting evolutionary optimization for avidity interactions. The combination of structure-based analysis of domain spacing with available monovalent experimental data appears, along with iterative experimental refinement of biophysical parameters, can identify high affinity interactions of tandem SH2 domain recruitment to the EGFR C-terminal tail. Using these principles, we extended bivalent predictions into the full phosphoproteome space and structural parameterization of other partners of SH2 domain binding, providing resources and methods for more rapid expansion of bivalent analysis. These approaches lay the groundwork for larger utility in multivalent prediction and testing to help better understand protein interactions that drive cell signaling.

BLI↗
PubMed2025

Structure-informed theoretical modeling defines principles governing avidity in bivalent protein interactions.

In signaling cascades, where domain-motif interactions tend to interact with relatively low affinity (allowing for reversibility), signaling proteins often encode multiple domains or motifs, which present the possibility of avidity - drastically increasing the interaction strength and duration as a result of multivalent binding. However, given the large combinatorial space, predicting and validating multivalent interactions that interact with avidity is a challenge. Here, we integrate mechanistic modeling, structure-based analysis, and experimental approaches as a framework for defining the conditions under which avidity plays a role. We explore the tandem SH2 domain family of interactions with bisphosphorylated partners as a multivalent archetype, which encompasses key secondary messengers in tyrosine kinase signaling networks. While certain multivalent interactions have been shown to be necessary in immune receptor recruitment of partners, bivalent recruitment of tandem SH2 domains more broadly is poorly understood. Theoretical modeling suggests that maximum avidity occurs with closely spaced or flexibly linked phosphotyrosine sites, combined with moderate monovalent affinities - exactly around the innate range of SH2 domain affinity. Surprisingly, despite sequence diversity, structure-based analysis showed remarkably conserved three-dimensional spacing between SH2 domains across all tandem SH2 families, which we corroborate experimentally, suggesting evolutionary optimization for avidity interactions. The combination of structure-based analysis of domain spacing with available monovalent experimental data appears to be sufficiently accurate to predict and rank order high affinity interactions of tandem SH2 domain recruitment to the EGFR C-terminal tail. These approaches lay the groundwork for larger utility in multivalent prediction and testing to help better understand protein interactions that drive cell signaling.

BLI↗