The STAR RNA binding proteins GLD-1, QKI, SAM68 and SLM-2 bind bipartite RNA motifs |
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| Authors: | André Galarneau and Stéphane Richard |
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| Institution: | (1) Terry Fox Molecular Oncology Group and the Bloomfield Center for Research on Aging, Lady Davis Institute for Medical Research, Sir Mortimer B. Davis Jewish General Hospital, and Departments of Oncology and Medicine, McGill University, Montr?al, Qu?bec, Canada, H3T 1E2;(2) Current address: Schering-Plough Canada Inc, Kirkland, QC, H9H 4M7, Canada;(3) Segal Cancer Centre, 3755 C?te Ste-Catherine Road, Montr?al, Qu?bec, Canada, H3T 1E2 |
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| Abstract: | Background SAM68, SAM68-like mammalian protein 1 (SLM-1) and 2 (SLM-2) are members of the K homology (KH) and STAR (signal transduction
activator of RNA metabolism) protein family. The function of these RNA binding proteins has been difficult to elucidate mainly
because of lack of genetic data providing insights about their physiological RNA targets. In comparison, genetic studies in
mice and C. elegans have provided evidence as to the physiological mRNA targets of QUAKING and GLD-1 proteins, two other members of the STAR
protein family. The GLD-1 binding site is defined as a hexanucleotide sequence (NACUCA) that is found in many, but not all,
physiological GLD-1 mRNA targets. Previously by using Systematic Evolution of Ligands by EXponential enrichment (SELEX), we defined the QUAKING binding site as a hexanucleotide sequence with an additional half-site
(UAAY). This sequence was identified in QKI mRNA targets including the mRNAs for myelin basic proteins. |
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