First published online October 17, 2002; 10.1104/pp.010280
Plant Physiol, November 2002, Vol. 130, pp. 1309-1318
Characterization of a NifS-Like Chloroplast Protein from
Arabidopsis. Implications for Its Role in Sulfur and Selenium
Metabolism1
Elizabeth A.H.
Pilon-Smits,*
Gulnara F.
Garifullina,
Salah
Abdel-Ghany,
Shin-Ichiro
Kato,
Hisaaki
Mihara,
Kerry L.
Hale,
Jason L.
Burkhead,
Nobuyoshi
Esaki,
Tatsuo
Kurihara, and
Marinus
Pilon
Biology Department, Colorado State University, Fort Collins,
Colorado 80523 (E.A.H.P.-S., G.F.G., S.A.-G., K.L.H., J.L.B., M.P.);
and Institute for Chemical Research, Kyoto University, Uji, Kyoto
611-0011, Japan (S.-I.K., H.M., N.E., T.K.)
NifS-like proteins catalyze the formation of elemental
sulfur (S) and alanine from cysteine (Cys) or of elemental selenium (Se) and alanine from seleno-Cys. Cys desulfurase activity is required to produce the S of iron (Fe)-S clusters, whereas seleno-Cys lyase activity is needed for the incorporation of Se in selenoproteins. In plants, the chloroplast is the location of (seleno) Cys formation and a location of Fe-S cluster formation. The goal of these studies was
to identify and characterize chloroplast NifS-like proteins. Using
seleno-Cys as a substrate, it was found that 25% to 30% of the NifS
activity in green tissue in Arabidopsis is present in chloroplasts. A
cDNA encoding a putative chloroplast NifS-like protein, AtCpNifS, was
cloned, and its chloroplast localization was confirmed using immunoblot
analysis and in vitro import. AtCpNIFS is expressed in
all major tissue types. The protein was expressed in Escherichia
coli and purified. The enzyme contains a pyridoxal 5' phosphate
cofactor and is a dimer. It is a type II NifS-like protein, more
similar to bacterial seleno-Cys lyases than to Cys desulfurases. The
enzyme is active on both seleno-Cys and Cys but has a much higher
activity toward the Se substrate. The possible role of AtCpNifS in
plastidic Fe-S cluster formation or in Se metabolism is discussed.
1
This work was supported by the U.S. National
Science Foundation (NSF; grant nos. MCB-9982432 to E.A.H.P.-S. and
MCB-0091163 to M.P.). The international collaborative research was
supported by the NSF (supplement to grant no. MCB9982432) and by a
Grant-in-aid for Joint Research Projects between Japan and the United
States from the Japan Society for the Promotion of Science (to
T.K.).
*
Corresponding author; e-mail epsmits{at}lamar.colostate.edu; fax
970-491-0649.
© 2002 American Society of Plant Biologists
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