Isolation of genomic and cDNA clones encoding bovine poly(A) binding protein II

Annette Nemeth, Sabine Krause, Diana Blank, Andreas Jenny, Paul Jenö, Ariel Lustig, Elmar Wahle

Research output: Contribution to journalArticlepeer-review

76 Scopus citations

Abstract

cDNA clones for bovine poly(A) binding protein II (PAB II) were isolated. Their sequence predicts a protein of 32.8 kDa, revising earlier estimates of molecular mass. The protein contains one putative RNA-binding domain of the RNP type, an acidic N-terminal and a basic C-terminal domain. Analyses of authentic PAB II were in good agreement with all predictions from the cDNA sequence except that a number of arginine residues appeared to be post-translationally modified. Poly(A) binding protein II expressed in Escherichia coli was active in poly(A) binding and reconstitution of processive polyadenylation, including poly(A) tail length control. The cDNA clones showed a number of potential PAB II binding sites in the 3′ untranslated sequence. Bovine poly(A)+ RNA contained two mRNAs hybridizing to a PAB II-specific probe. Analysis of a genomic clone revealed six introns in the coding sequence. The revised molecular mass led to a demonstration of PAB II oligomer formation and a reinterpretation of earlier data concerning the protein's binding to poly(A).

Original languageEnglish (US)
Pages (from-to)4034-4041
Number of pages8
JournalNucleic acids research
Volume23
Issue number20
DOIs
StatePublished - Oct 25 1995

ASJC Scopus subject areas

  • Genetics

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