A role for mrgA, a DPS family protein, in the internal transport of Fe in the cyanobacterium Synechocystis sp PCC6803

被引:73
作者
Skolnick, Sigal
Yeala, Shaked B.
Keren, Nir
机构
[1] Hebrew Univ Jerusalem, Alexander Silberman Inst Life Sci, Dept Plant & Environm Sci, IL-91904 Jerusalem, Israel
[2] Hebrew Univ Jerusalem, Inter Univ Inst Marine Sci, IL-91904 Jerusalem, Israel
[3] Hebrew Univ Jerusalem, Inst Earth Sci, IL-91904 Jerusalem, Israel
来源
BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS | 2007年 / 1767卷 / 06期
关键词
cyanobacteria; DPS family protein; Fe; Synechocystis sp;
D O I
10.1016/j.bbabio.2006.11.015
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The mrgA protein of the cyanobacterium Synechocystsis sp. PCC6803 is a member of the DPS Fe storage protein family. The physiological role of this protein was studied using a disruption mutant in the mrgA gene (slr1894) and by measuring intracellular Fe quotas, 77K chlorophyll fluorescence and growth rates. It was found that the deletion of the mrgA gene did not impair the Fe storage capacity, as the intracellular Fe quotas of the Delta mrgA cells were comparable to those of the wild type. Furthermore, the cellular response to decreasing external Fe concentrations, as detected by the emergence of the CP43' 77K fluorescence band, was similar in wild type and mutant cultures. On the other hand, a considerable slow down in the growth rate of Delta mrgA cultures was observed upon transfer from Fe replete to Fe depleted medium, indicating impeded utilization of the plentiful intracellular Fe. Based on these results, we suggest that mrgA plays an important role in the transport of intracellular Fe from storage (within bacterioferritins) to biosynthesis of metal cofactors throughout the cell's growth. (c) 2006 Elsevier B.V All rights reserved.
引用
收藏
页码:814 / 819
页数:6
相关论文
共 26 条
[1]   SIMPLE CONDITIONS FOR GROWTH OF UNICELLULAR BLUE-GREEN ALGAE ON PLATES [J].
ALLEN, MM .
JOURNAL OF PHYCOLOGY, 1968, 4 (01) :1-&
[2]   Bacterial iron homeostasis [J].
Andrews, SC ;
Robinson, AK ;
Rodríguez-Quiñones, F .
FEMS MICROBIOLOGY REVIEWS, 2003, 27 (2-3) :215-237
[3]   Overexpression and characterization of an iron storage and DNA-binding Dps protein from Trichodesmium erythraeum [J].
Castruita, M ;
Saito, M ;
Schottel, PC ;
Elmegreen, LA ;
Myneni, S ;
Stiefel, EI ;
Morel, FMM .
APPLIED AND ENVIRONMENTAL MICROBIOLOGY, 2006, 72 (04) :2918-2924
[4]   METALLOREGULATION IN BACILLUS-SUBTILIS - ISOLATION AND CHARACTERIZATION OF 2 GENES DIFFERENTIALLY REPRESSED BY METAL-IONS [J].
CHEN, L ;
JAMES, LP ;
HELMANN, JD .
JOURNAL OF BACTERIOLOGY, 1993, 175 (17) :5428-5437
[5]  
Durham KA, 2002, J BASIC MICROB, V42, P367, DOI 10.1002/1521-4028(200212)42:6<367::AID-JOBM367>3.0.CO
[6]  
2-T
[7]   Transition metal speciation in the cell: Insights from the chemistry of metal ion receptors [J].
Finney, LA ;
O'Halloran, TV .
SCIENCE, 2003, 300 (5621) :931-936
[8]   Genes essential to iron transport in the cyanobacterium Synechocystis sp strain PCC 6803 [J].
Katoh, H ;
Hagino, N ;
Grossman, AR ;
Ogawa, T .
JOURNAL OF BACTERIOLOGY, 2001, 183 (09) :2779-2784
[9]   Critical roles of bacterioferritins in iron storage and proliferation of cyanobacteria [J].
Keren, N ;
Aurora, R ;
Pakrasi, HB .
PLANT PHYSIOLOGY, 2004, 135 (03) :1666-1673
[10]   A light-dependent mechanism for massive accumulation of manganese in the photosynthetic bacterium Synechocystis sp PCC 6803 [J].
Keren, N ;
Kidd, MJ ;
Penner-Hahn, JE ;
Pakrasi, HB .
BIOCHEMISTRY, 2002, 41 (50) :15085-15092