Purification and characterization of Ku-2, an octamer-binding protein related to the autoantigen Ku

The octamer motif (ATTTGCAT) is an important regulatory element in eukaryotic gene expression. A previously unidentified protein that recognizes this motif has been isolated from the human B cell line, Daudi. The protein, which we term Ku-2, bears a close resemblance to the DNA-binding autoantigen Ku. Like Ku, it is a heterodimer with subunits of 83 and 72 kDa; antisera raised against either subunit of Ku cross-react with Ku-2. Two peptides have been sequenced and show a strong similarity to regions in the corresponding subunits of Ku. The sequences are not identical, however, suggesting that Ku-2 may be a B cell homologue of Ku. Both Ku and Ku-2 bind to the termini of DNA duplexes, but Ku-2 also binds to an internal octamer motif. It is not known whether Ku shares the latter property or whether the octamer binding is a consequence of sequence differences between the two proteins. Ku-2 does not react with antisera against the POU domain of the octamer-binding protein Oct-2, indicating that the DNA binding domains of the two proteins are dissimilar despite the ability of both to bind to the octamer motif. We discuss the evidence for the existence of a family of octamer-binding proteins related to Ku.     

Xenopus laevis Oct-1 does not bind to certain histone H2B gene promoter octamer motifs for which a novel octamer-binding factor has high affinity.

Oct-1 and a second, previously unidentified octamer-binding protein (Oct-R) have been identified in extracts of Xenopus laevis oocytes and embryos. Oct-1 does not bind to the octamer motif associated with certain Xenopus laevis histone H2B gene promoters, whereas Oct-R binds well to this motif, but only in the sequence context of the H2B gene promoter.