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Structure and function of nematode RNA-binding proteins

Journal

CURRENT OPINION IN STRUCTURAL BIOLOGY
Volume 20, Issue 3, Pages 305-312

Publisher

CURRENT BIOLOGY LTD
DOI: 10.1016/j.sbi.2010.03.010

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Funding

  1. NIH [R01 GM081422]
  2. March of Dimes

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RNA-binding proteins are critical effectors of gene expression. They guide mRNA localization, translation, and stability, and potentially play a role in regulating mRNA synthesis. The structural basis for RNA recognition by RNA-binding proteins is the key to understand how they target specific transcripts for regulation. Compared to other metazoans, nematode genomes contain a significant expansion in several RNA-binding protein families, including Pumilio-FBF (PUF), UP-like zinc finger (TZF), and Argonaute-like (AGO) proteins. Genetic data suggest that individual members of each family have distinct functions, presumably due to sequence variations that alter RNA-binding specificity or protein interaction partners. In this review, we highlight example structures and identify the variable regions that likely contribute to functional divergence in nematodes.

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