Interaction of rat poly(A)-binding protein with poly(A)- and non-poly(A) sequences is preferentially mediated by RNA recognition motifs 3+4.
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.
Mullin
Carola
C
Department for Cell Biochemistry and Clinical Neurobiology, University Hospital Hamburg-Eppendorf, Martinistrasse 52, 20246 Hamburg, Germany.
Duning
Kerstin
K
Barnekow
Angelika
A
Richter
Dietmar
D
Kremerskothen
Joachim
J
Mohr
Evita
E
D000818:Animals; D001665:Binding Sites; D002460:Cell Line; D007700:Kinetics; D008969:Molecular Sequence Data; D016296:Mutagenesis; D011061:Poly A / Q000378:metabolism*; D039102:Poly(A)-Binding Proteins / Q000378:metabolism*; D012313:RNA / Q000737:chemistry* / Q000378:metabolism*; D051381:Rats; D011994:Recombinant Proteins / Q000378:metabolism; D017384:Sequence Deletion; D013379:Substrate Specificity; D014162:Transfection
D039102:Poly(A)-Binding Proteins; D011994:Recombinant Proteins; D011061:Poly A; D012313:RNA