Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease

Research output: Contribution to journalArticle

Standard

Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease. / Pettinati, Ilaria; Grzechnik, Pawel; de Almeida, Claudia Ribeiro; Brem, Jurgen; McDonough, Michael A.; Dhir, Somdutta; Proudfoot, Nick J.; Schofield, Christopher J.

In: Elife, Vol. 7, e39865, 03.12.2018.

Research output: Contribution to journalArticle

Harvard

Pettinati, I, Grzechnik, P, de Almeida, CR, Brem, J, McDonough, MA, Dhir, S, Proudfoot, NJ & Schofield, CJ 2018, 'Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease', Elife, vol. 7, e39865. https://doi.org/10.7554/eLife.39865

APA

Pettinati, I., Grzechnik, P., de Almeida, C. R., Brem, J., McDonough, M. A., Dhir, S., Proudfoot, N. J., & Schofield, C. J. (2018). Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease. Elife, 7, [e39865]. https://doi.org/10.7554/eLife.39865

Vancouver

Pettinati I, Grzechnik P, de Almeida CR, Brem J, McDonough MA, Dhir S et al. Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease. Elife. 2018 Dec 3;7. e39865. https://doi.org/10.7554/eLife.39865

Author

Pettinati, Ilaria ; Grzechnik, Pawel ; de Almeida, Claudia Ribeiro ; Brem, Jurgen ; McDonough, Michael A. ; Dhir, Somdutta ; Proudfoot, Nick J. ; Schofield, Christopher J. / Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease. In: Elife. 2018 ; Vol. 7.

Bibtex

@article{029afbaeb8824d3a84f2afd2c45cbb34,
title = "Biosynthesis of histone messenger RNA employs a specific 3{\textquoteright} end endonuclease",
abstract = "Replication-dependent (RD) core histone mRNA produced during S-phase is the only known metazoan protein-coding mRNA presenting a 3{\textquoteright} stem-loop instead of the otherwise universal polyA tail. A metallo b-lactamase (MBL) fold enzyme, cleavage and polyadenylation specificity factor 73 (CPSF73), is proposed to be the sole endonuclease responsible for 3{\textquoteright} 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{\textquoteright} 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.",
author = "Ilaria Pettinati and Pawel Grzechnik and {de Almeida}, {Claudia Ribeiro} and Jurgen Brem and McDonough, {Michael A.} and Somdutta Dhir and Proudfoot, {Nick J.} and Schofield, {Christopher J.}",
year = "2018",
month = dec,
day = "3",
doi = "10.7554/eLife.39865",
language = "English",
volume = "7",
journal = "Elife",
issn = "2050-084X",
publisher = "eLife Sciences Publications",

}

RIS

TY - JOUR

T1 - Biosynthesis of histone messenger RNA employs a specific 3’ end endonuclease

AU - Pettinati, Ilaria

AU - Grzechnik, Pawel

AU - de Almeida, Claudia Ribeiro

AU - Brem, Jurgen

AU - McDonough, Michael A.

AU - Dhir, Somdutta

AU - Proudfoot, Nick J.

AU - Schofield, Christopher J.

PY - 2018/12/3

Y1 - 2018/12/3

N2 - 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 b-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.

AB - 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 b-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.

UR - http://www.scopus.com/inward/record.url?scp=85058876097&partnerID=8YFLogxK

U2 - 10.7554/eLife.39865

DO - 10.7554/eLife.39865

M3 - Article

C2 - 30507380

AN - SCOPUS:85058876097

VL - 7

JO - Elife

JF - Elife

SN - 2050-084X

M1 - e39865

ER -