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Biochemical and structural studies of conserved Maf proteins revealed nucleotide pyrophosphatases with a preference for modified nucleotides.
- Source :
-
Chemistry & biology [Chem Biol] 2013 Nov 21; Vol. 20 (11), pp. 1386-98. Date of Electronic Publication: 2013 Oct 24. - Publication Year :
- 2013
-
Abstract
- 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.<br /> (Copyright © 2013 The Authors. Published by Elsevier Ltd.. All rights reserved.)
- Subjects :
- Bacillus subtilis enzymology
Conserved Sequence
Crystallography, X-Ray
Escherichia coli enzymology
Humans
Maf Transcription Factors genetics
Models, Molecular
Mutagenesis, Site-Directed
Saccharomyces cerevisiae enzymology
Salmonella typhimurium enzymology
Salmonella typhimurium genetics
Substrate Specificity
Escherichia coli Proteins metabolism
Maf Transcription Factors chemistry
Maf Transcription Factors metabolism
Nucleotides chemistry
Nucleotides metabolism
Pyrophosphatases metabolism
Subjects
Details
- Language :
- English
- ISSN :
- 1879-1301
- Volume :
- 20
- Issue :
- 11
- Database :
- MEDLINE
- Journal :
- Chemistry & biology
- Publication Type :
- Academic Journal
- Accession number :
- 24210219
- Full Text :
- https://doi.org/10.1016/j.chembiol.2013.09.011