Journal
CHEMISTRY & BIOLOGY
Volume 20, Issue 11, Pages 1386-1398Publisher
CELL PRESS
DOI: 10.1016/j.chembiol.2013.09.011
Keywords
-
Categories
Funding
- Government of Canada through Genome Canada
- Ontario Genomics Institute [2009-OGI-ABC-1405, OGI-055]
- Ontario Research Fund [ORFGL2-01-004]
- COMBREX
- UK Medical Research Council [MC_U105192716]
- Natural Sciences and Engineering Research Council
- Canadian Institutes of Health Research
- National Institutes of Health [P50GM071508, 1R01CA16359-01A1]
- Canada Foundation for Innovation
- Eli Lilly Canada
- GlaxoSmithKline
- Ontario Ministry of Economic Development and Innovation
- Novartis Research Foundation
- Pfizer
- AbbVie
- Takeda
- Janssen
- Boehringer Ingelheim
- Wellcome Trust
- Medical Research Council [MC_U105192716] Funding Source: researchfish
- MRC [MC_U105192716] Funding Source: UKRI
Ask authors/readers for more resources
Maf (for multicopy associated filamentation) proteins represent a large family of conserved proteins implicated in cell division arrest but whose biochemical activity remains unknown. Here, we show that the prokaryotic and eukaryotic Maf proteins exhibit nucleotide pyrophosphatase activity against 5-methyl-UTP, pseudo-UTP, 5-methyl-CTP, and 7-methyl-GTP, which represent the most abundant modified bases in all organisms, as well as against canonical nucleotides dTTP, UTP, and CTP. Overexpression of the Maf protein YhdE. in E. coli cells increased intracellular levels of dTMP and UMP, confirming that dTTP and UTP are the in vivo substrates of this protein. Crystal structures and site-directed mutagenesis of Maf proteins revealed the determinants of their activity and substrate specificity. Thus, pyrophosphatase activity of Maf proteins toward canonical and modified nucleotides might provide the molecular mechanism for a dual role of these proteins in cell division arrest and house cleaning.
Authors
I am an author on this paper
Click your name to claim this paper and add it to your profile.
Reviews
Recommended
No Data Available