Abstract
In immunogold double-labeling of pea leaf thin sections with antibodies raised against ferredoxin-NADP reductase (EC 1.18.1.2, FNR) and antibodies directed against the A or B subunits of the NADP-linked glyceraldehyde-3-P dehydrogenase (GAPD) (EC 1.2.1.13), many small and large gold particles were found together over the chloroplasts. Nearest neighbor analysis of the distribution of the gold particles indicates that FNR and the NADP-linked GAPD are co-localized, in situ. This suggests that FNR might carry FADH2 or NADPH from the thylakoid membrane to GAPD, or that ferredoxin might carry electrons to FNR co-localized with GAPD in the stroma. Crystal structures of the spinach enzymes are available. When they are docked computationally, the proteins appear, as modeled, to be able to form at least two different complexes. One involves a single GAPD monomer and an FNR monomer (or dimer). The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer (or dimer). The interface residues are conserved in this model as well. Ferredoxin is able to interact with FNR in either complex.
| Original language | English (US) |
|---|---|
| Pages (from-to) | 18-30 |
| Number of pages | 13 |
| Journal | Journal of Structural Biology |
| Volume | 161 |
| Issue number | 1 |
| DOIs | |
| State | Published - Jan 2008 |
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Keywords
- Co-localization
- Ferredoxin-NADP reductase
- Glyceraldehyde-3-P dehydrogenase
- Nearest neighbor analysis
- Photosynthetic CO-fixation
- Pisum sativum
ASJC Scopus subject areas
- Structural Biology
Cite this
Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts. / Negi, Surendra S.; Carol, Andrew A.; Pandya, Shivangi; Braun, Werner; Anderson, Louise E.
In: Journal of Structural Biology, Vol. 161, No. 1, 01.2008, p. 18-30.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Co-localization of glyceraldehyde-3-phosphate dehydrogenase with ferredoxin-NADP reductase in pea leaf chloroplasts
AU - Negi, Surendra S.
AU - Carol, Andrew A.
AU - Pandya, Shivangi
AU - Braun, Werner
AU - Anderson, Louise E.
PY - 2008/1
Y1 - 2008/1
N2 - In immunogold double-labeling of pea leaf thin sections with antibodies raised against ferredoxin-NADP reductase (EC 1.18.1.2, FNR) and antibodies directed against the A or B subunits of the NADP-linked glyceraldehyde-3-P dehydrogenase (GAPD) (EC 1.2.1.13), many small and large gold particles were found together over the chloroplasts. Nearest neighbor analysis of the distribution of the gold particles indicates that FNR and the NADP-linked GAPD are co-localized, in situ. This suggests that FNR might carry FADH2 or NADPH from the thylakoid membrane to GAPD, or that ferredoxin might carry electrons to FNR co-localized with GAPD in the stroma. Crystal structures of the spinach enzymes are available. When they are docked computationally, the proteins appear, as modeled, to be able to form at least two different complexes. One involves a single GAPD monomer and an FNR monomer (or dimer). The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer (or dimer). The interface residues are conserved in this model as well. Ferredoxin is able to interact with FNR in either complex.
AB - In immunogold double-labeling of pea leaf thin sections with antibodies raised against ferredoxin-NADP reductase (EC 1.18.1.2, FNR) and antibodies directed against the A or B subunits of the NADP-linked glyceraldehyde-3-P dehydrogenase (GAPD) (EC 1.2.1.13), many small and large gold particles were found together over the chloroplasts. Nearest neighbor analysis of the distribution of the gold particles indicates that FNR and the NADP-linked GAPD are co-localized, in situ. This suggests that FNR might carry FADH2 or NADPH from the thylakoid membrane to GAPD, or that ferredoxin might carry electrons to FNR co-localized with GAPD in the stroma. Crystal structures of the spinach enzymes are available. When they are docked computationally, the proteins appear, as modeled, to be able to form at least two different complexes. One involves a single GAPD monomer and an FNR monomer (or dimer). The amino acid residues located at the putative interface are highly conserved on the chloroplastic forms of both enzymes. The other potential complex involves the GAPD A2B2 tetramer and an FNR monomer (or dimer). The interface residues are conserved in this model as well. Ferredoxin is able to interact with FNR in either complex.
KW - Co-localization
KW - Ferredoxin-NADP reductase
KW - Glyceraldehyde-3-P dehydrogenase
KW - Nearest neighbor analysis
KW - Photosynthetic CO-fixation
KW - Pisum sativum
UR - http://www.scopus.com/inward/record.url?scp=37349023392&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=37349023392&partnerID=8YFLogxK
U2 - 10.1016/j.jsb.2007.08.016
DO - 10.1016/j.jsb.2007.08.016
M3 - Article
C2 - 17945509
AN - SCOPUS:37349023392
VL - 161
SP - 18
EP - 30
JO - Journal of Structural Biology
JF - Journal of Structural Biology
SN - 1047-8477
IS - 1
ER -