New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942

Pietsch D, Bernat G, Kahmann U, Staiger D, Pistorius EK, Michel K-P (2011)
Photosynthesis Research 108(2-3): 121-132.

Journal Article | Published | English

No fulltext has been uploaded

Author
; ; ; ; ;
Abstract
Iron limitation has a strong impact on electron transport reactions of the unicellular fresh water cyanobacterium Synechococcus elongatus PCC 7942 (thereafter referred to as S.elongatus). Among the various adaptational processes on different cellular levels, iron limitation induces a strongly enhanced expression of IdiC (iron-deficiency-induced protein C). In this article, we show that IdiC is loosely attached to the thylakoid and to the cytoplasmic membranes and that its expression is enhanced during conditions of iron starvation and during the late growth phase. The intracellular IdiC level was even more increased when additional iron was replenished in the late growth phase. On the basis of its amino acid sequence and of its absorbance spectrum, IdiC can be classified as a member of the family of thioredoxin (TRX)-like (2Fe-2S) ferredoxins. The presence of an iron cofactor in IdiC was detected by inductive coupled plasma optical emission spectrometry (ICP-OES). Comparative measurements of electron transport activities of S.elongatus wild type (WT) and an IdiC-merodiploid mutant called MuD, which contained a strongly reduced IdiC content under iron-sufficient as well as iron-deficient growth conditions, were performed. The results revealed that MuD had a strongly increased light sensitivity, especially under iron limitation. The measurements of photosystem II (PS II)-mediated electron transport rates in WT and MuD strain showed that PS II activity was significantly lower in MuD than in the WT strain. Moreover, P(700) (+) re-reduction rates provided evidence that the respiratory activities, which were very low in the MuD strain in the presence of iron, significantly increased in iron-starved cells. Thus, an increase in respiration may compensate for the drastic decrease of photosynthetic electron transport activity in MuD grown under iron starvation. Based on the similarity of the S. elongatus IdiC to the NuoE subunit of the NDH-1 complex in Escherichia coli, it is likely that IdiC has a function in the electron transport processes from NAD(P)H to the plastoquinone pool. This is in agreement with the up-regulation of IdiC in the late growth phase as well as under stress conditions when PS II is damaged. As absence or high reduction of the IdiC level would prevent or reduce the formation of functional NDH-1 complexes, under such conditions electron transport routes via alternative substrate dehydrogenases, donating electrons to the plastoquinone pool, can be assumed to be up-regulated.
Publishing Year
ISSN
eISSN
PUB-ID

Cite this

Pietsch D, Bernat G, Kahmann U, Staiger D, Pistorius EK, Michel K-P. New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942. Photosynthesis Research. 2011;108(2-3):121-132.
Pietsch, D., Bernat, G., Kahmann, U., Staiger, D., Pistorius, E. K., & Michel, K. - P. (2011). New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942. Photosynthesis Research, 108(2-3), 121-132.
Pietsch, D., Bernat, G., Kahmann, U., Staiger, D., Pistorius, E. K., and Michel, K. - P. (2011). New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942. Photosynthesis Research 108, 121-132.
Pietsch, D., et al., 2011. New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942. Photosynthesis Research, 108(2-3), p 121-132.
D. Pietsch, et al., “New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942”, Photosynthesis Research, vol. 108, 2011, pp. 121-132.
Pietsch, D., Bernat, G., Kahmann, U., Staiger, D., Pistorius, E.K., Michel, K.-P.: New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942. Photosynthesis Research. 108, 121-132 (2011).
Pietsch, Daniel, Bernat, Gabor, Kahmann, Uwe, Staiger, Dorothee, Pistorius, Elfriede K, and Michel, Klaus-Peter. “New insights into the function of the iron deficiency-induced protein C from Synechococcus elongatus PCC 7942”. Photosynthesis Research 108.2-3 (2011): 121-132.
This data publication is cited in the following publications:
This publication cites the following data publications:

2 Citations in Europe PMC

Data provided by Europe PubMed Central.

Methyl viologen responsive proteome dynamics of Anabaena sp. strain PCC7120.
Panda B, Basu B, Rajaram H, Kumar Apte S., Proteomics 14(16), 2014
PMID: 24946113

50 References

Data provided by Europe PubMed Central.


KP, Z Naturforsch C 47(), 1992

KP, Physiol Plant 119(), 2004
Molecular characterization of idiA and adjacent genes in the cyanobacteria Synechococcus sp. strains PCC 6301 and PCC 7942.
Michel KP, Kruger F, Puhler A, Pistorius EK., Microbiology (Reading, Engl.) 145 ( Pt 6)(), 1999
PMID: 10411274
Transcript profiling reveals new insights into the acclimation of the mesophilic fresh-water cyanobacterium Synechococcus elongatus PCC 7942 to iron starvation.
Nodop A, Pietsch D, Hocker R, Becker A, Pistorius EK, Forchhammer K, Michel KP., Plant Physiol. 147(2), 2008
PMID: 18424627

T, Arch Microbiol 139(), 1984
Characterization of the putative iron sulfur protein IdiC (ORF5) in Synechococcus elongatus PCC 7942.
Pietsch D, Staiger D, Pistorius EK, Michel KP., Photosyn. Res. 94(1), 2007
PMID: 17690995
Some properties of a basic L-amino-acid oxidase from Anacystis nidulans.
Pistorius EK, Voss H., Biochim. Biophys. Acta 611(2), 1980
PMID: 6766743

G, Photosynth Res 6(), 1985
Iron stress responses in the cyanobacterium Synechococcus sp. PCC7942.
Sandstrom S, Ivanov AG, Park YI, Oquist G, Gustafsson P., Physiol Plant 116(2), 2002
PMID: 12354203
Detection of an L-amino acid dehydrogenase activity in Synechocystis sp. PCC 6803.
Schriek S, Kahmann U, Staiger D, Pistorius EK, Michel KP., J. Exp. Bot. 60(3), 2009
PMID: 19213808
Crystal structure of Pasteurella haemolytica ferric ion-binding protein A reveals a novel class of bacterial iron-binding proteins.
Shouldice SR, Dougan DR, Williams PA, Skene RJ, Snell G, Scheibe D, Kirby S, Hosfield DJ, McRee DE, Schryvers AB, Tari LW., J. Biol. Chem. 278(42), 2003
PMID: 12882966
Novel anion-independent iron coordination by members of a third class of bacterial periplasmic ferric ion-binding proteins.
Shouldice SR, McRee DE, Dougan DR, Tari LW, Schryvers AB., J. Biol. Chem. 280(7), 2005
PMID: 15576371

AUTHOR UNKNOWN, 0
Localization and function of the IdiA homologue Slr1295 in the cyanobacterium Synechocystis sp. strain PCC 6803.
Tolle J, Michel KP, Kruip J, Kahmann U, Preisfeld A, Pistorius EK., Microbiology (Reading, Engl.) 148(Pt 10), 2002
PMID: 12368463
Anion-independent iron coordination by the Campylobacter jejuni ferric binding protein.
Tom-Yew SA, Cui DT, Bekker EG, Murphy ME., J. Biol. Chem. 280(10), 2005
PMID: 15613474
Multiple Rieske proteins enable short- and long-term light adaptation of Synechocystis sp. PCC 6803.
Tsunoyama Y, Bernat G, Dyczmons NG, Schneider D, Rogner M., J. Biol. Chem. 284(41), 2009
PMID: 19674969
PsaE Is Required for in Vivo Cyclic Electron Flow around Photosystem I in the Cyanobacterium Synechococcus sp. PCC 7002.
Yu L, Zhao J, Muhlenhoff U, Bryant DA, Golbeck JH., Plant Physiol. 103(1), 1993
PMID: 12231924

Export

0 Marked Publications

Open Data PUB

Web of Science

View record in Web of Science®

Sources

PMID: 21607697
PubMed | Europe PMC

Search this title in

Google Scholar