Structure of an active human histone pre-mRNA 3′-end processing machinery

Author:

Sun Yadong1ORCID,Zhang Yixiao2ORCID,Aik Wei Shen1ORCID,Yang Xiao-Cui3,Marzluff William F.34ORCID,Walz Thomas2,Dominski Zbigniew34ORCID,Tong Liang1ORCID

Affiliation:

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

2. Laboratory of Molecular Electron Microscopy, Rockefeller University, New York, NY 10065, USA.

3. Integrative Program for Biological and Genome Sciences, University of North Carolina at Chapel Hill, Chapel Hill, NC 27599, USA.

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

Abstract

Architecture of an mRNA processor The 3′-end processing of the three major classes of RNA polymerase II transcripts in metazoan cells—polyadenylated messenger RNAs (mRNAs), histone mRNAs, and small nuclear RNAs (snRNAs)—requires three distinct machineries that share common features. Sun et al. reconstituted the active human histone pre-mRNA 3′-end processing machinery and solved its structure at near-atomic resolution by cryo–electron microscopy. This structure provides a basis for understanding the mechanism of the shared catalytic reactions between histone pre-mRNA and canonical pre-mRNA and snRNA 3′-end processing machineries. Science , this issue p. 700

Funder

National Institute of General Medical Sciences

Publisher

American Association for the Advancement of Science (AAAS)

Subject

Multidisciplinary

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