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EMBO reports 9, 10, 1013–1018 (2008)
doi:10.1038/embor.2008.146
AOP Published online: 8 August 2008
Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3'-end maturation
Nikolay G Kolev1, 2, Therese A Yario1, 2, Eleni Benson2† & Joan A Steitz1, 2
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1 Howard Hughes Medical Institute, and
2 Department of Molecular Biophysics and Biochemistry, Yale University, 295 Congress Avenue, New Haven, Connecticut 06519, USA
To whom correspondence should be addressed
Joan A Steitz Tel: +1 203 737 4418; Fax: +1 203 624 8213; E-mail: joan.steitz@yale.edu
† Present address: Baylor College of Medicine, BCM368, One Baylor Plaza, Houston, Texas 77030, USA
Received 7 May 2008; Accepted 1 July 2008; Published online 8 August 2008.
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Abstract
In eukaryotes, the process of messenger RNA 3'-end formation involves endonucleolytic cleavage of the transcript followed by synthesis of the poly(A) tail. The complex machinery involved in this maturation process contains two proteins of the metallo- -lactamase (MBL) superfamily, the 73 and 100 kDa subunits of the cleavage and polyadenylation specificity factor (CPSF). By using an in vitro system to assess point mutations in these two mammalian proteins, we found that conserved residues from the MBL motifs of both polypeptides are required for assembly of the endonuclease activity that cleaves histone pre-mRNAs. This indicates that CPSF73 and CPSF100 act together in the process of maturation of eukaryotic pre-messenger RNAs, similar to other members of the MBL family, RNases Z and J, which function as homodimers.
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