Structure of Histone mRNA Stem-Loop, Human Stem-Loop Binding Protein, and 3′hExo Ternary Complex

Author:

Tan Dazhi1,Marzluff William F.23,Dominski Zbigniew23,Tong Liang1

Affiliation:

1. Department of Biological Sciences, Columbia University, New York, NY 10027, USA.

2. Department of Biochemistry and Biophysics, University of North Carolina, Chapel Hill, NC 27599, USA.

3. Program in Molecular Biology and Biotechnology, University of North Carolina, Chapel Hill, NC 27599, USA.

Abstract

Recognizing a Stem-Loop Structure Metazoan histone messenger RNAs (mRNAs) have a conserved stem-loop (SL) structure at their 3′-end. The stem-loop is bound by the stem-loop binding protein (SLBP), which is required for histone mRNA 3′-end processing, export, stability, and translation. The 3′-5′ exonuclease 3′hExo also binds the SL and trims off three nucleotides. Tan et al. (p. 318 ) determined the high-resolution structure of the SL bound by the RNA-binding domain (RBD) of human SLBP together with human 3′hExo. The conformation of the loop differed substantially from other RNA tetraloops and the SLBP RBD may function as a ruler that can measure the length of the stem. Although the SLBP directly recognizes the guanine base of the second nucleotide of the stem, it appears that SLBP and 3′hExo recognize the unique shape of the SL.

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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