Skip to main content
U.S. Department of Energy
Office of Scientific and Technical Information

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

Journal Article · · Proceedings of the National Academy of Sciences of the United States of America; (United States)
;  [1]; ;  [2]
  1. Columbia Univ., New York, NY (United States)
  2. Princeton Univ., NJ (United States)
Cleavage stimulation factor is one of the multiple factors required for 3{prime}-end cleavage of mammalian pre-mRNAs. The authors 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-cross linked to RNA in a polyadenylylation signal (AAUAAA)-dependent manner. They 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 {alpha}-helix stabilized by salt bridges is predicted. An {approx}270-amino acid segment surrounding this repeat structure is highly enriched in proline and glycine residues ({approx}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.
OSTI ID:
5482477
Journal Information:
Proceedings of the National Academy of Sciences of the United States of America; (United States), Journal Name: Proceedings of the National Academy of Sciences of the United States of America; (United States) Vol. 89:4; ISSN 0027-8424; ISSN PNASA
Country of Publication:
United States
Language:
English