The human 64-kDa polyadenylylation factor contains a ribonucleoprotein- type RNA binding domain and unusual auxiliary motifs

Y. Takagaki, C. C. MacDonald, T. Shenk, J. L. Manley

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Abstract

Cleavage stimulation factor is one of the multiple factors required for 3'-end cleavage of mammalian pre-mRNAs. We have shown previously that this factor is composed of three subunits with estimated molecular masses of 77, 64, and 50 kDa and that the 64-kDa subunit can be UV-crosslinked to RNA in a polyadenylylation signal (AAUAAA)-dependent manner. We have now isolated cDNAs encoding the 64-kDa subunit of human cleavage stimulation factor. The 64-kDa subunit contains a ribonucleoprotein-type RNA binding domain in the N- terminal region and a repeat structure in the C-terminal region in which a pentapeptide sequence (consensus MEARA/G) is repeated 12 times and the formation of a long α-helix stabilized by salt bridges is predicted. An ≃270-amino acid segment surrounding this repeat structure is highly enriched in proline and glycine residues (≃20% for each). When cloned 64-kDa subunit was expressed in Escherichia coli, an N-terminal fragment containing the RNA binding domain bound to RNAs in a polyadenylylation-signal-independent manner, suggesting that the RNA binding domain is directly involved in the binding of the 64-kDa subunit to pre-mRNAs.

Original languageEnglish (US)
Pages (from-to)1403-1407
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume89
Issue number4
DOIs
StatePublished - 1992

All Science Journal Classification (ASJC) codes

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