Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942

Stork T, Laxa M, Dietz MS, Dietz K-J (2009)
ARCHIVES OF MICROBIOLOGY 191(2): 141-151.

Download
Es wurde kein Volltext hochgeladen. Nur Publikationsnachweis!
Zeitschriftenaufsatz | Veröffentlicht | Englisch
Autor
; ; ;
Abstract / Bemerkung
The genome of Synechococcus elongatus PCC 7942 encodes six peroxiredoxins (Prx). Single genes are present each for a 1-Cys Prx and a 2-Cys Prx, while four genes code for PrxQ-like proteins (prxQ-A1, -A2, -A3 and B). Their transcript accumulation varies with growth conditions in a gene-specific manner (Stork et al. in J Exp Bot 56:3193-3206, 2005). To address their functional properties, members of the prx gene family were produced as recombinant proteins and analysed for their peroxide detoxification capacity and quaternary structure by size exclusion chromatography. Independent of the reduction state, the 2-Cys Prx separated as oligomer, the 1-Cys Prx as dimer and the PrxQ-A1 as monomer. PrxQ-A2 was inactive in our assays, 1-Cys Prx activity was unaffected by addition of TrxA, while all others were stimulated to a variable extent by addition of E. coli thioredoxin. Sensitivity towards cumene hydroperoxide treatment of E. coli BL21 cells expressing the cyanobacterial PrxQ-A1 to A3 proteins was greatly reduced, while expression of the other Prx had no effect. The study shows differentiation of Prx functions in S. elongatus PCC 7942 which is discussed in relation to potential roles in site- and stress-specific defence.
Erscheinungsjahr
Zeitschriftentitel
ARCHIVES OF MICROBIOLOGY
Band
191
Ausgabe
2
Seite(n)
141-151
ISSN
eISSN
PUB-ID

Zitieren

Stork T, Laxa M, Dietz MS, Dietz K-J. Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942. ARCHIVES OF MICROBIOLOGY. 2009;191(2):141-151.
Stork, T., Laxa, M., Dietz, M. S., & Dietz, K. - J. (2009). Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942. ARCHIVES OF MICROBIOLOGY, 191(2), 141-151. doi:10.1007/s00203-008-0438-7
Stork, T., Laxa, M., Dietz, M. S., and Dietz, K. - J. (2009). Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942. ARCHIVES OF MICROBIOLOGY 191, 141-151.
Stork, T., et al., 2009. Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942. ARCHIVES OF MICROBIOLOGY, 191(2), p 141-151.
T. Stork, et al., “Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942”, ARCHIVES OF MICROBIOLOGY, vol. 191, 2009, pp. 141-151.
Stork, T., Laxa, M., Dietz, M.S., Dietz, K.-J.: Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942. ARCHIVES OF MICROBIOLOGY. 191, 141-151 (2009).
Stork, Tina, Laxa, Miriam, Dietz, Marina S., and Dietz, Karl-Josef. “Functional characterisation of the peroxiredoxin gene family members of Synechococcus elongatus PCC 7942”. ARCHIVES OF MICROBIOLOGY 191.2 (2009): 141-151.

11 Zitationen in Europe PMC

Daten bereitgestellt von Europe PubMed Central.

Expression of OsTPX Gene Improves Cellular Redox Homeostasis and Photosynthesis Efficiency in Synechococcus elongatus PCC 7942.
Kim YS, Kim JJ, Park SI, Diamond S, Boyd JS, Taton A, Kim IS, Golden JW, Yoon HS., Front Plant Sci 9(), 2018
PMID: 30619416
Characterization of a bacterioferritin comigratory protein family 1-Cys peroxiredoxin from Candidatus Liberibacter asiaticus.
Singh A, Kumar N, Tomar PPS, Bhose S, Ghosh DK, Roy P, Sharma AK., Protoplasma 254(4), 2017
PMID: 27987036
Peroxiredoxins are conserved markers of circadian rhythms.
Edgar RS, Green EW, Zhao Y, van Ooijen G, Olmedo M, Qin X, Xu Y, Pan M, Valekunja UK, Feeney KA, Maywood ES, Hastings MH, Baliga NS, Merrow M, Millar AJ, Johnson CH, Kyriacou CP, O'Neill JS, Reddy AB., Nature 485(7399), 2012
PMID: 22622569
The cellular energization state affects peripheral stalk stability of plant vacuolar H+-ATPase and impairs vacuolar acidification.
Schnitzer D, Seidel T, Sander T, Golldack D, Dietz KJ., Plant Cell Physiol 52(5), 2011
PMID: 21474463
Peroxiredoxins in plants and cyanobacteria.
Dietz KJ., Antioxid Redox Signal 15(4), 2011
PMID: 21194355
Structural and biochemical characterization of peroxiredoxin Qbeta from Xylella fastidiosa: catalytic mechanism and high reactivity.
Horta BB, de Oliveira MA, Discola KF, Cussiol JR, Netto LE., J Biol Chem 285(21), 2010
PMID: 20335172
The oligomeric conformation of peroxiredoxins links redox state to function.
Barranco-Medina S, Lázaro JJ, Dietz KJ., FEBS Lett 583(12), 2009
PMID: 19464293

51 References

Daten bereitgestellt von Europe PubMed Central.


S, Biochem 47(), 2008
Peroxynitrite reductase activity of bacterial peroxiredoxins.
Bryk R, Griffin P, Nathan C., Nature 407(6801), 2000
PMID: 11001062
Thioredoxin-linked "thiol peroxidase" from periplasmic space of Escherichia coli.
Cha MK, Kim HK, Kim IH., J. Biol. Chem. 270(48), 1995
PMID: 7499381
Cloning, sequencing, and mutation of thiol-specific antioxidant gene of Saccharomyces cerevisiae.
Chae HZ, Kim IH, Kim K, Rhee SG., J. Biol. Chem. 268(22), 1993
PMID: 8344960
The Arabidopsis plastidial thioredoxins: new functions and new insights into specificity.
Collin V, Issakidis-Bourguet E, Marchand C, Hirasawa M, Lancelin JM, Knaff DB, Miginiac-Maslow M., J. Biol. Chem. 278(26), 2003
PMID: 12707279
Plant peroxiredoxins.
Dietz KJ., Annu Rev Plant Biol 54(), 2003
PMID: 14502986

KJ, 2005
The function of peroxiredoxins in plant organelle redox metabolism.
Dietz KJ, Jacob S, Oelze ML, Laxa M, Tognetti V, de Miranda SM, Baier M, Finkemeier I., J. Exp. Bot. 57(8), 2006
PMID: 16606633

EF, 1990

AUTHOR UNKNOWN, 0
The mitochondrial type II peroxiredoxin F is essential for redox homeostasis and root growth of Arabidopsis thaliana under stress.
Finkemeier I, Goodman M, Lamkemeyer P, Kandlbinder A, Sweetlove LJ, Dietz KJ., J. Biol. Chem. 280(13), 2005
PMID: 15632145
Peroxiredoxins.
Hofmann B, Hecht HJ, Flohe L., Biol. Chem. 383(3-4), 2002
PMID: 12033427

F, Plant Physiol Biochem 40(), 2002
Divergent light-, ascorbate-, and oxidative stress-dependent regulation of expression of the peroxiredoxin gene family in Arabidopsis.
Horling F, Lamkemeyer P, Konig J, Finkemeier I, Kandlbinder A, Baier M, Dietz KJ., Plant Physiol. 131(1), 2003
PMID: 12529539
Anti-oxidative stress system in cyanobacteria. Significance of type II peroxiredoxin and the role of 1-Cys peroxiredoxin in Synechocystis sp. strain PCC 6803.
Hosoya-Matsuda N, Motohashi K, Yoshimura H, Nozaki A, Inoue K, Ohmori M, Hisabori T., J. Biol. Chem. 280(1), 2004
PMID: 15509585
Sequence analysis of the genome of the unicellular cyanobacterium Synechocystis sp. strain PCC6803. II. Sequence determination of the entire genome and assignment of potential protein-coding regions (supplement).
Kaneko T, Sato S, Kotani H, Tanaka A, Asamizu E, Nakamura Y, Miyajima N, Hirosawa M, Sugiura M, Sasamoto S, Kimura T, Hosouchi T, Matsuno A, Muraki A, Nakazaki N, Naruo K, Okumura S, Shimpo S, Takeuchi C, Wada T, Watanabe A, Yamada M, Yasuda M, Tabata S., DNA Res. 3(3), 1996
PMID: 8905238
Response to oxidative stress involves a novel peroxiredoxin gene in the unicellular cyanobacterium Synechocystis sp. PCC 6803.
Kobayashi M, Ishizuka T, Katayama M, Kanehisa M, Bhattacharyya-Pakrasi M, Pakrasi HB, Ikeuchi M., Plant Cell Physiol. 45(3), 2004
PMID: 15047877

OA, Microbiol 75(), 2006
Reaction mechanism of plant 2-Cys peroxiredoxin. Role of the C terminus and the quaternary structure.
Konig J, Lotte K, Plessow R, Brockhinke A, Baier M, Dietz KJ., J. Biol. Chem. 278(27), 2003
PMID: 12702727
Peroxiredoxin Q of Arabidopsis thaliana is attached to the thylakoids and functions in context of photosynthesis.
Lamkemeyer P, Laxa M, Collin V, Li W, Finkemeier I, Schottler MA, Holtkamp V, Tognetti VB, Issakidis-Bourguet E, Kandlbinder A, Weis E, Miginiac-Maslow M, Dietz KJ., Plant J. 45(6), 2006
PMID: 16507087

Y, Proc Natl Acad Sci USA 101(), 2004
Glutathionylation induces the dissociation of 1-Cys D-peroxiredoxin non-covalent homodimer.
Noguera-Mazon V, Lemoine J, Walker O, Rouhier N, Salvador A, Jacquot JP, Lancelin JM, Krimm I., J. Biol. Chem. 281(42), 2006
PMID: 16916801
Thinking about the evolution of photosynthesis.
Olson JM, Blankenship RE., Photosyn. Res. 80(1-3), 2004
PMID: 16328834
The Prx Q protein of Arabidopsis thaliana is a member of the luminal chloroplast proteome.
Petersson UA, Kieselbach T, Garcia-Cerdan JG, Schroder WP., FEBS Lett. 580(26), 2006
PMID: 17054949
Thioredoxin peroxidases of the malarial parasite Plasmodium falciparum.
Rahlfs S, Becker K., Eur. J. Biochem. 268(5), 2001
PMID: 11231293
Bacterial RNA isolation with one hour centrifugation in a table-top ultracentrifuge.
Reddy KJ, Webb R, Sherman LA., BioTechniques 8(3), 1990
PMID: 1691916
Isolation and characterization of a new peroxiredoxin from poplar sieve tubes that uses either glutaredoxin or thioredoxin as a proton donor.
Rouhier N, Gelhaye E, Sautiere PE, Brun A, Laurent P, Tagu D, Gerard J, de Fay E, Meyer Y, Jacquot JP., Plant Physiol. 127(3), 2001
PMID: 11706208
Poplar peroxiredoxin Q. A thioredoxin-linked chloroplast antioxidant functional in pathogen defense.
Rouhier N, Gelhaye E, Gualberto JM, Jordy MN, De Fay E, Hirasawa M, Duplessis S, Lemaire SD, Frey P, Martin F, Manieri W, Knaff DB, Jacquot JP., Plant Physiol. 134(3), 2004
PMID: 14976238
Functional complementation in yeast reveals a protective role of chloroplast 2-Cys peroxiredoxin against reactive nitrogen species.
Sakamoto A, Tsukamoto S, Yamamoto H, Ueda-Hashimoto M, Takahashi M, Suzuki H, Morikawa H., Plant J. 33(5), 2003
PMID: 12609026
Evidence for genetic transformation in blue-green alga Anacystis nidulans.
Shestakov SV, Khyen NT., Mol. Gen. Genet. 107(4), 1970
PMID: 4999302

DP, Z Naturforsch 55(), 2000
Lipid peroxidation as a source of oxidative damage in Helicobacter pylori: protective roles of peroxiredoxins.
Wang G, Hong Y, Johnson MK, Maier RJ., Biochim. Biophys. Acta 1760(11), 2006
PMID: 17069977
Molecular evidence for the early evolution of photosynthesis.
Xiong J, Fischer WM, Inoue K, Nakahara M, Bauer CE., Science 289(5485), 2000
PMID: 10976061
Thioredoxin peroxidase in the Cyanobacterium Synechocystis sp. PCC 6803.
Yamamoto H, Miyake C, Dietz KJ, Tomizawa K, Murata N, Yokota A., FEBS Lett. 447(2-3), 1999
PMID: 10214959

Export

Markieren/ Markierung löschen
Markierte Publikationen

Open Data PUB

Web of Science

Dieser Datensatz im Web of Science®

Quellen

PMID: 18974976
PubMed | Europe PMC

Suchen in

Google Scholar