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Abstract Organisms from all kingdoms of life depend on Late Embryogenesis Abundant (LEA) proteins to survive desiccation. LEA proteins are divided into broad families distinguished by the presence of family‐specific motif sequences. The LEA_4 family, characterized by 11‐residue motifs, plays a crucial role in the desiccation tolerance of numerous species. However, the role of these motifs in the function of LEA_4 proteins is unclear, with some studies finding that they recapitulate the function of full‐length LEA_4 proteins in vivo, and other studies finding the opposite result. In this study, we characterize the ability of LEA_4 motifs to protect a desiccation‐sensitive enzyme, citrate synthase (CS), from loss of function during desiccation. We show here that LEA_4 motifs not only prevent the loss of function of CS during desiccation but also that they can do so more robustly via synergistically interactions with cosolutes. Our analysis further suggests that cosolutes induce synergy with LEA_4 motifs in a manner that correlates with transfer free energy. This research advances our understanding of LEA_4 proteins by demonstrating that during desiccation their motifs can protect specific clients to varying degrees and that their protective capacity is modulated by their chemical environment. Our findings extend beyond the realm of desiccation tolerance, offering insights into the interplay between IDPs and cosolutes. By investigating the function of LEA_4 motifs, we highlight broader strategies for understanding protein stability and function. 

We introduce a novel sufficient dimension-reduction (SDR) method which is robust against outliers using α-distance covariance (dCov)in dimension-reduction problems. Under very mild conditions on the predictors, the central subspace is effectively estimated and model-free without estimating link function based on the projection on the Stiefel manifold. We establish the convergence property of the pro-posed estimation under some regularity conditions. We compare the performance of our method with existing SDR methods by simulation and real data analysis and show that our algorithm improves the computational efficiency and effectiveness. 

While matrix-covariate regression models have been studied in many existing works, classical statistical and computational methods for the analysis of the regression coefficient estimation are highly affected by high dimensional matrix-valued covariates. To address these issues, this paper proposes a framework of matrix-covariate regression models based on a low-rank constraint and an additional regularization term for structured signals, with considerations of models of both continuous and binary responses. We propose an efficient Riemannian-steepest-descent algorithm for regression coefficient estimation. We prove that the consistency of the proposed estimator is in the order of O(sqrt{r(q+m)+p}/sqrt{n}), where r is the rank, p x m is the dimension of the coefficient matrix and p is the dimension of the coefficient vector. When the rank r is small, this rate improves over O(sqrt{qm+p}/sqrt{n}), the consistency of the existing work (Li et al. in Electron J Stat 15:1909-1950, 2021) that does not apply a rank constraint. In addition, we prove that all accumulation points of the iterates have similar estimation errors asymptotically and substantially attaining the minimax rate. We validate the proposed method through a simulated dataset on two-dimensional shape images and two real datasets of brain signals and microscopic leucorrhea images. 

Abstract To survive extreme drying (anhydrobiosis), many organisms, spanning every kingdom of life, accumulate intrinsically disordered proteins (IDPs). For decades, the ability of anhydrobiosis‐related IDPs to form transient amphipathic helices has been suggested to be important for promoting desiccation tolerance. However, evidence empirically supporting the necessity and/or sufficiency of helicity in mediating anhydrobiosis is lacking. Here, we demonstrate that the linker region of CAHS D, a desiccation‐related IDP from the tardigradeHypsibius exemplaris, that contains significant helical structure, is the protective portion of this protein. Perturbing the sequence composition and grammar of the linker region of CAHS D, through the insertion of helix‐breaking prolines, modulating the identity of charged residues, or replacement of hydrophobic amino acids with serine or glycine residues results in variants with different degrees of helical structure. Importantly, correlation of protective capacity and helical content in variants generated through different helix perturbing modalities does not show as strong a trend, suggesting that while helicity is important, it is not the only property that makes a protein protective during desiccation. These results provide direct evidence for the decades‐old theory that helicity of desiccation‐related IDPs is linked to their anhydrobiotic capacity.