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Conserved motifs in both CPSF73 and CPSF100 are required to assemble the active endonuclease for histone mRNA 3′‐end maturation
Author(s) -
Kolev Nikolay G,
Yario Therese A,
Benson Eleni,
Steitz Joan A
Publication year - 2008
Publication title -
embo reports
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 4.584
H-Index - 184
eISSN - 1469-3178
pISSN - 1469-221X
DOI - 10.1038/embor.2008.146
Subject(s) - polyadenylation , cleavage and polyadenylation specificity factor , biology , messenger rna , endonuclease , histone , precursor mrna , rna binding protein , rna , conserved sequence , microbiology and biotechnology , sequence motif , genetics , rna splicing , dna , gene , peptide sequence
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‐β‐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.