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Manganese is a Deinococcus radiodurans growth limiting factor in rich culture medium.

Authors :
Borsetti F
Dal Piaz F
D'Alessio F
Stefan A
Brandimarti R
Sarkar A
Datta A
Montón Silva A
den Blaauwen T
Alberto M
Spisni E
Hochkoeppler A
Source :
Microbiology (Reading, England) [Microbiology (Reading)] 2018 Oct; Vol. 164 (10), pp. 1266-1275. Date of Electronic Publication: 2018 Jul 27.
Publication Year :
2018

Abstract

To understand the effects triggered by Mn <superscript>2+</superscript> on Deinococcus radiodurans, the proteome patterns associated with different growth phases were investigated. In particular, under physiological conditions we tested the growth rate and the biomass yield of D. radiodurans cultured in rich medium supplemented or not with MnCl2. The addition of 2.5-5.0 µM MnCl2 to the medium neither altered the growth rate nor the lag phase, but significantly increased the biomass yield. When higher MnCl2 concentrations were used (10-250 µM), biomass was again found to be positively affected, although we did observe a concentration-dependent lag phase increase. The in vivo concentration of Mn <superscript>2+</superscript> was determined in cells grown in rich medium supplemented or not with 5 µM MnCl2. By atomic absorption spectroscopy, we estimated 0.2 and 0.75 mM Mn <superscript>2+</superscript> concentrations in cells grown in control and enriched medium, respectively. We qualitatively confirmed this observation using a fluorescent turn-on sensor designed to selectively detect Mn <superscript>2+</superscript> in vivo. Finally, we investigated the proteome composition of cells grown for 15 or 19 h in medium to which 5 µM MnCl2 was added, and we compared these proteomes with those of cells grown in the control medium. The presence of 5 µM MnCl2 in the culture medium was found to alter the pI of some proteins, suggesting that manganese affects post-translational modifications. Further, we observed that Mn <superscript>2+</superscript> represses enzymes linked to nucleotide recycling, and triggers overexpression of proteases and enzymes linked to the metabolism of amino acids.

Details

Language :
English
ISSN :
1465-2080
Volume :
164
Issue :
10
Database :
MEDLINE
Journal :
Microbiology (Reading, England)
Publication Type :
Academic Journal
Accession number :
30052171
Full Text :
https://doi.org/10.1099/mic.0.000698