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Research Paper
Poly(A)-Binding Protein Binds to A-Rich Sequences via RNA-Binding Domains 1+2 and 3+4
Tasneem Khanam, Ravi Sondekoppa Muddashetty, Avak Kahvejian, Nahum Sonenberg and Juergen Brosius
volume 3 | issue 4
october/november/december 2006Pages: 170 - 177
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Poly(A) binding protein (PABP) binds non-protein-coding BC1 RNA and BC200 RNA, which contain adenosine-rich domains. Two combinations of the four PABP RNA recognition motifs (RRMs), RRMs 1+2 and RRMs 3+4, bind with very strong affinities to various transcripts with long stretches of adenosine residues, whereas RRMs 2+3 bind weakly. While RRMs 1+2 preferentially bind to stretches that contain only adenosines, RRMs 3+4 exhibit relatively high affinities towards sequences that are interspersed with other nucleotides. Binding studies with oligoribonucleotide(A)65 and oligoribonucleotide(A)25 showed that the shorter RNA is not an ideal substrate for binding studies to model the interactions with mRNAs, which in general harbor long poly(A) tails.
Authors
Tasneem Khanam
Institute of Experimental Pathology, ZMBE, University of Münster; Münster, Germany
Ravi Sondekoppa Muddashetty
Institute of Experimental Pathology, ZMBE, University of Münster; Münster, Germany
Avak Kahvejian
Department of Biochemistry and McGill Cancer Center, McGill University; Montreal, Quebec, Canada
Nahum Sonenberg
Department of Biochemistry and McGill Cancer Center, McGill University; Montreal, Quebec, Canada
Juergen Brosius
Institute of Experimental Pathology, ZMBE, University of Münster; Münster, Germany
We now provide open access to journal articles published online for one year or more. This article may be downloaded at the following link:
Download PDF If the document does not open, please right-click on the link (control-click on a Macintosh) and select the option to save the file to disk.