Publications by authors named "S Sukenik"

Mutations in genomic DNA often result in single-point missense mutations in proteins. For folded proteins, the functional effect of these missense mutations can often be understood by their impact on structure. However, missense mutations in intrinsically disordered protein regions (IDRs) remain poorly understood.

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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.

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Transcription factor proteins bind to specific DNA promoter sequences and initiate gene transcription. These proteins often contain intrinsically disordered activation domains (ADs) that regulate their transcriptional activity. Like other disordered protein regions, ADs do not have a fixed three-dimensional structure and instead exist in an ensemble of conformations.

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The conformational ensemble and function of intrinsically disordered proteins (IDPs) are sensitive to their solution environment. The inherent malleability of disordered proteins, combined with the exposure of their residues, accounts for this sensitivity. One context in which IDPs play important roles that are concomitant with massive changes to the intracellular environment is during desiccation (extreme drying).

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Article Synopsis
  • Transcription factors bind to DNA and kickstart gene transcription, often featuring disordered regions called activation domains (ADs) that affect their functionality.
  • These ADs don’t have a fixed shape; instead, they exist in multiple conformations that are influenced by their amino acid sequences.
  • In a study measuring the structural dimensions of two ADs (HIF-1α and CITED2) using FRET microscopy, it was found that altering the shape of HIF-1α influenced its ability to activate transcription, while CITED2's activity remained unaffected by its structural changes.
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