Structure of a nucleotide-bound Clp1Pcf11 polyadenylation factor

Structure of a nucleotide-bound Clp1Pcf11 polyadenylation factor,10.1093/nar/gkl1010,Nucleic Acids Research,Christian G. Noble,Barbara Beuth,Ian A. Ta

Structure of a nucleotide-bound Clp1Pcf11 polyadenylation factor   (Citations: 13)
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Pcf11 and Clp1 are subunits of cleavage factor IA (CFIA), an essential polyadenylation factor in Saccahromyces cerevisiae. We have determined the structure of a ternary complex of Clp1 together with ATP and the Clp1-binding region of Pcf11. Clp1 contains three domains, a small N-terminal b sandwich domain, a C-terminal domain containing a novel a/b-fold and a central domain that binds ATP. The arrangement of the nucleotide binding site is similar to that observed in SIMIBI-class ATPase subunits found in other multisubunit macromolecu- lar complexes. However, despite this similarity, nucleotide hydrolysis does not occur. The Pcf11 binding site is also located in the central domain where three highly conserved residues in Pcf11 mediate many of the protein-protein interactions. We propose that this conserved Clp1-Pcf11 inter- action is responsible for maintaining a tight cou- pling between the Clp1 nucleotide binding subunit and the other components of the polyadenylation machinery. Moreover, we suggest that this complex represents a stabilized ATP bound form of Clp1 that requires the participation of other non-CFIA processing factors in order to initiate timely ATP hydrolysis during 30 end processing.
Journal: Nucleic Acids Research - NAR , vol. 35, no. 1, pp. 87-99, 2006
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