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The Pab1p protein was discovered in Saccharomyces cerevisia since it is abundant and binds specifically to the polyA tails of mRNA molecules. The systematic name in the Saccharomyces genome database is YER165w. It has a role in polyA length control in combination with Nab2p and may also be involved in mRNA stability and transcription. Pab1p is found in both the cytoplasm and nuclei of yeast cells and has a deduced molecular weight of 64 kDa, but runs on typical SDS-PAGE gels at about 67kDa. The yeast Pab1p protein sequence includes four RNA recognition motifs followed by a single C-terminal polyA binding domain. The closest human homolog of the yeast protein is polyadenylate-binding protein cytoplasmic 1-like (PABPC1L) which has the same domain structure, although is not well conserved in amino acid sequence. There are seven human genes encoding polyA binding proteins, four of which produce proteins with the same domain structure as yeast Pab1p and human PABPC1L.
Poly(A) binding protein