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The PUF Family of RNA‐binding Proteins: Does Evolutionarily Conserved Structure Equal Conserved Function?
Author(s) -
Spassov Danislav,
Jurecic Roland
Publication year - 2003
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1080/15216540310001603093
Subject(s) - conserved sequence , biology , rna binding protein , genetics , rna , protein family , microbiology and biotechnology , protein domain , untranslated region , peptide sequence , gene
Drosophila Pumilio ( Pum ) protein is a founder member of a novel family of RNA‐binding proteins, known as the PUF family. The PUF proteins constitute an evolutionarily highly conserved family of proteins present from yeast to humans and plants, and are characterized by a highly conserved C‐terminal RNA‐binding domain, composed of eight tandem repeats. The conserved biochemical features and genetic function of PUF family members have emerged from studies of model organisms. PUF proteins bind to related sequence motifs in the 3' untranslated region (3'UTR) of specific target mRNAs and repress their translation. Frequently, PUF proteins function asymmetrically to create protein gradients, thus causing asymmetric cell division and regulating cell fate specification. Thus, it was recently proposed that the primordial role of PUF proteins is to sustain mitotic proliferation of stem cells. Here we review the evolution, conserved genetic and biochemical properties of PUF family of proteins, and discuss protein interactions, upstream regulators and downstream targets of PUF proteins. We also suggest that a conserved mechanism of PUF function extends to the newly described mammalian members of the PUF family (human PUM1 and PUM2, and mouse Pum1 and Pum2 ), that show extensive homology to Drosophila Pum, and could have an important role in cell development, fate specification and differentiation. IUBMB Life, 55: 359‐366, 2003