Biosynthesis of histone messenger RNA employs a specific 3' end endonuclease.

Abstract:

:Replication-dependent (RD) core histone mRNA produced during S-phase is the only known metazoan protein-coding mRNA presenting a 3' stem-loop instead of the otherwise universal polyA tail. A metallo β-lactamase (MBL) fold enzyme, cleavage and polyadenylation specificity factor 73 (CPSF73), is proposed to be the sole endonuclease responsible for 3' end processing of both mRNA classes. We report cellular, genetic, biochemical, substrate selectivity, and crystallographic studies providing evidence that an additional endoribonuclease, MBL domain containing protein 1 (MBLAC1), is selective for 3' processing of RD histone pre-mRNA during the S-phase of the cell cycle. Depletion of MBLAC1 in cells significantly affects cell cycle progression thus identifying MBLAC1 as a new type of S-phase-specific cancer target.

journal_name

Elife

journal_title

eLife

authors

Pettinati I,Grzechnik P,Ribeiro de Almeida C,Brem J,McDonough MA,Dhir S,Proudfoot NJ,Schofield CJ

doi

10.7554/eLife.39865

subject

Has Abstract

pub_date

2018-12-03 00:00:00

issn

2050-084X

pii

39865

journal_volume

7

pub_type

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