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Interaction of rat poly(A)‐binding protein with poly(A)‐ and non‐poly(A) sequences is preferentially mediated by RNA recognition motifs 3 + 4
Author(s) -
Mullin Carola,
Duning Kerstin,
Barnekow Angelika,
Richter Dietmar,
Kremerskothen Joachim,
Mohr Evita
Publication year - 2004
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/j.febslet.2004.09.054
Subject(s) - rna , messenger rna , rna binding protein , rna recognition motif , poly(a) binding protein , chemistry , binding site , microbiology and biotechnology , biology , biochemistry , gene
Vasopressin (VP) mRNA and the non‐coding BC200 RNA are sorted to neuronal dendrites. Among proteins interacting specifically with both RNAs is the multifunctional poly(A)‐binding protein (PABP) consisting of four RNA recognition motifs (RRMs) and a C‐terminal auxiliary domain. The protein/RNA interaction studies presented here reveal that PABPs association with VP‐ and BC200 RNA is exclusively mediated by RRMs 3 + 4. Quantitative binding studies with PABP deletion mutants demonstrate preferential binding of RRMs 3 + 4 even to poly(A)‐homopolymers, while RRMs 1 + 2 exhibit a lower affinity for those sequences. An optimal interaction with both poly(A)‐ and non‐poly(A) sequences is only achieved by full‐size PABP.